Transient Inhibition of Translation Initiation by Osmotic Stress

Abstract

Cells respond and adapt to changes in the environment. In this study, we examined the effect of environmental stresses on protein synthesis in the yeast Saccharomyces cerevisiae. We found that osmotic stress causes irreversible inhibition of methionine uptake, transient inhibition of uracil uptake, transient stimulation of glucose uptake, transient repression of ribosomal protein (RP) genes such as CYH2 andRPS27, and the transient inhibition of translation initiation. Rapid inhibition of translation initiation by osmotic stress requires a novel pathway, different from the amino acid-sensing pathway, the glucose-sensing pathway, and the TOR pathway. The Hog1 MAP kinase pathway is not involved in the inhibition of either methionine uptake or translation initiation but is required for the adaptation of translation initiation after inhibition and the repression of RP genes by osmotic stress. These results suggest that the transient inhibition of translation initiation occurs as a result of a combination of both acute inhibition of translation and the long-term activation of translation by the Hog1 pathway. Cells respond and adapt to changes in the environment. In this study, we examined the effect of environmental stresses on protein synthesis in the yeast Saccharomyces cerevisiae. We found that osmotic stress causes irreversible inhibition of methionine uptake, transient inhibition of uracil uptake, transient stimulation of glucose uptake, transient repression of ribosomal protein (RP) genes such as CYH2 andRPS27, and the transient inhibition of translation initiation. Rapid inhibition of translation initiation by osmotic stress requires a novel pathway, different from the amino acid-sensing pathway, the glucose-sensing pathway, and the TOR pathway. The Hog1 MAP kinase pathway is not involved in the inhibition of either methionine uptake or translation initiation but is required for the adaptation of translation initiation after inhibition and the repression of RP genes by osmotic stress. These results suggest that the transient inhibition of translation initiation occurs as a result of a combination of both acute inhibition of translation and the long-term activation of translation by the Hog1 pathway. Translation is governed by the interaction of a number of different structural elements of mRNAs and the translation machinery. In eukaryotes, regulation of translation is carried out by distinct factors that interact with specific regions in the individual mRNA sequence, mostly the 5′ or the 3′ untranslated region. General regulation is exercised via the modulation of the components of the translation machinery, which interact with common regions including the 5′ cap, the coding region, and poly(A) tail structures (1.McCarthy J.E.G. Microbiol. Mol. Biol. Rev. 1998; 62: 1492-1553Crossref PubMed Google Scholar, 2.Pain V.M. Eur. J. Biochem. 1996; 236: 747-771Crossref PubMed Scopus (638) Google Scholar). For general regulation of translation initiation, many signals, such as serum, PDGF, insulin, phorbol ester, EGF, and others, stimulate translation in eukaryotic cells. Other signals, such as virus infection, vasopressin, heat shock, and deprivation of serum or amino acids, are known to inhibit translation initiation in eukaryotes (2.Pain V.M. Eur. J. Biochem. 1996; 236: 747-771Crossref PubMed Scopus (638) Google Scholar,3.Kleijn M. Scheper G.C. Voorma H.O. Thomas A.A. Eur. J. Biochem. 1998; 253: 531-544Crossref PubMed Scopus (169) Google Scholar). In the yeast Saccharomyces cerevisiae, nutrient limitation is known to be an strong general regulator of translation initiation (1.McCarthy J.E.G. Microbiol. Mol. Biol. Rev. 1998; 62: 1492-1553Crossref PubMed Google Scholar, 4.Ashe M.P. De Long S.K. Sachs A.B. Mol. Biol. Cell. 2000; 11: 833-848Crossref PubMed Scopus (314) Google Scholar). Depriving yeast of amino acids or purines inhibits translation initiation through the phosphorylation pathway of the α-subunit of eIF2, a translation initiation factor (1.McCarthy J.E.G. Microbiol. Mol. Biol. Rev. 1998; 62: 1492-1553Crossref PubMed Google Scholar, 5.Hinnebusch A.G. J. Biol. Chem. 1997; 272: 21661-21664Abstract Full Text Full Text PDF PubMed Scopus (434) Google Scholar). The immunosuppressant rapamycin binds with the immunophilin FKBP and inhibits the TOR 1The abbreviations used are: TORtarget of rapamycinHOGhigh osmolarity glycerolMAPKmitogen-activated protein kinaseMAPKKKMAPK kinase kinaseRPribosomal proteinprotein (a target of rapamycin), which is related to phosphatidylinositol-3 kinase. This results in the inhibition of translation initiation, and growth is arrested in early G1 phase. Loss of the TOR function also causes translational inhibition and induces physiological changes characteristic of nutrient-starved G0 cells. Thus, the TOR kinase controls cell growth by sensing environmental nutrients (6.Barbet N.C. Schneider U. Helliwell S.B. Stansfield I. Tuite M.F. Hall M.N. Mol. Biol. Cell. 1996; 7: 25-42Crossref PubMed Scopus (603) Google Scholar, 7.Heitman J. Movva N.R. Hall M.N. Science. 1991; 253: 905-909Crossref PubMed Scopus (1562) Google Scholar, 8.Helliwell S.B. Wagner P. Kunz J. Deuter-Reinhard M. Henriquez R. Hall M.N. Mol. Biol. Cell. 1994; 5: 105-118Crossref PubMed Scopus (317) Google Scholar). Recently, it has been reported that glucose deprivation rapidly inhibits translation initiation through the glucose repression pathway or the protein kinase A pathway (4.Ashe M.P. De Long S.K. Sachs A.B. Mol. Biol. Cell. 2000; 11: 833-848Crossref PubMed Scopus (314) Google Scholar). However, signals other than the nutrient signals described above could also be involved in the general regulation of translation initiation. target of rapamycin high osmolarity glycerol mitogen-activated protein kinase MAPK kinase kinase ribosomal protein S. cerevisiae cells respond to increases in external osmolarity by regulating amino acid uptake, protein synthesis (9.Varela J.C. van Beekvelt C. Planta R.J. Mager W.H. Mol. Microbiol. 1992; 6: 2183-2190Crossref PubMed Scopus (92) Google Scholar), the activity of the solute transporter (10.Luyten K. Albertyn J. Skibbe W.F. Prior B.A. Ramos J. Thevelein J.M. Hohmann S. EMBO J. 1995; 14: 1360-1371Crossref PubMed Scopus (337) Google Scholar, 11.Tamas M.J. Luyten K. Sutherland F.C. Hernandez A. Albertyn J. Valadi H. Li H. Prior B.A. Kilian S.G. Ramos J. Gustafsson L. Thevelein J.M. Hohmann S. Mol. Microbiol. 1999; 31: 1087-1104Crossref PubMed Scopus (295) Google Scholar), the expression of many genes (12.Posas F. Chambers J.R. Heyman J.A. Hoeffler J.P. de Nadal E. Arino J. J. Biol. Chem. 2000; 275: 17249-17255Abstract Full Text Full Text PDF PubMed Scopus (335) Google Scholar, 13.Gasch A.P. Spellman P.T. Kao C.M. Carmel-Harel O. Eisen M.B. Gisela S. Botstein D. Brown P.O. Mol. Biol. Cell. 2000; 11: 4241-4257Crossref PubMed Scopus (3762) Google Scholar, 14.Causton H.C. Ren B. Koh S.S. Harbison C.T. Kanin E. Jennings E.G. Lee T.I. True H.L. Lander E.S. Young R.A. Mol. Biol. Cell. 2001; 12: 323-337Crossref PubMed Scopus (1077) Google Scholar) including the genes involved in solute accumulation (15.Albertyn J. Hohmann S. Thevelein J.M. Prior B.A. Mol. Cell. Biol. 1994; 14: 4135-4144Crossref PubMed Scopus Google Scholar), and the of S. J. Biol. 1992; PubMed Scopus Google Scholar) and I. S. A. Microbiol. 2000; PubMed Scopus Google Scholar). These are to be required for adaptation to the growth The osmolarity pathway is known to be rapidly by high The pathway and on kinase kinase and the that in the activation of which in Hog1 MAPK de E. Science. PubMed Scopus Google Scholar, H. 1994; PubMed Scopus Google Scholar, M. H. Science. 1995; PubMed Scopus Google Scholar, F. H. Cell. 1996; Full Text Full Text PDF PubMed Scopus Google Scholar). The Hog1 MAPK pathway is for the expression of specific genes for adaptation to high such as which (15.Albertyn J. Hohmann S. Thevelein J.M. Prior B.A. Mol. Cell. Biol. 1994; 14: 4135-4144Crossref PubMed Scopus Google Scholar). Recently, has that the Hog1 MAPK pathway the expression of many genes in to to high osmolarity (12.Posas F. Chambers J.R. Heyman J.A. Hoeffler J.P. de Nadal E. Arino J. J. Biol. Chem. 2000; 275: 17249-17255Abstract Full Text Full Text PDF PubMed Scopus (335) Google Scholar). has been reported that osmotic stress inhibits nutrient uptake, protein and the expression of many genes including ribosomal protein (RP) genes (9.Varela J.C. van Beekvelt C. Planta R.J. Mager W.H. Mol. Microbiol. 1992; 6: 2183-2190Crossref PubMed Scopus (92) Google Scholar, 13.Gasch A.P. Spellman P.T. Kao C.M. Carmel-Harel O. Eisen M.B. Gisela S. Botstein D. Brown P.O. Mol. Biol. Cell. 2000; 11: 4241-4257Crossref PubMed Scopus (3762) Google Scholar, W.H. J.C. Mol. Microbiol. PubMed Scopus (92) Google Scholar). However, it which of translation are by osmotic and it is not known the Hog1 MAPK pathway to we the of osmotic stress on translation initiation and the of the Hog1 MAPK pathway in the regulation of nutrient uptake and RP expression as as translation initiation. The used in this are in I. in the by the with to the described by D. Botstein D. Science. PubMed Scopus Google used in this are in M. H. Science. 1995; PubMed Scopus Google M. H. Science. 1995; PubMed Scopus Google M. H. Science. 1995; PubMed Scopus Google M. H. Science. 1995; PubMed Scopus Google M. A. A. A. 1999; PubMed Scopus Google M. A. A. A. 1999; PubMed Scopus Google A.B. Cell. Full Text PDF PubMed Scopus Google Sachs A.B. Mol. Cell. Biol. 1997; PubMed Scopus Google Sachs A.B. Mol. Cell. Biol. 1997; PubMed Scopus Google D. R. A. Mol. Cell. Biol. PubMed Scopus Google J. S. M. Scopus Google J. S. M. Scopus Google A. M.P. S. EMBO J. 1998; PubMed Scopus Google are in in a and by the and CYH2 and that of of and that of The by the by M. and the by the of is a of the by A. Mol. Cell. Biol. 2000; PubMed Scopus Google Scholar). The by and as by of the the and the The by the of the that has the of to in and a of the 5′ the L. 6: PubMed Scopus Google Scholar). an by of and of Cells in yeast with or yeast with or the of to the cells the the of both uptake of methionine and protein synthesis by the (6.Barbet N.C. Schneider U. Helliwell S.B. Stansfield I. Tuite M.F. Hall M.N. Mol. Biol. Cell. 1996; 7: 25-42Crossref PubMed Scopus (603) Google Scholar). of in methionine and for with of For as a protein synthesis of the with the of acid and for by through a and with an of acid and with For the the of the with of on a and with an of These and a The uptake as the or the of The protein synthesis as the of to of the For of uracil uptake, the in with uracil for with of For of glucose uptake, the in yeast for with Cells in of the of or rapamycin (6.Barbet N.C. Schneider U. Helliwell S.B. Stansfield I. Tuite M.F. Hall M.N. Mol. Biol. Cell. 1996; 7: 25-42Crossref PubMed Scopus (603) Google Scholar) to the used in this For deprivation of amino acids or glucose the cells by and with or The cells in the used for and of and on for For to the to a of and the on for and and of by with S.B. F. Mol. Cell. Biol. 5: PubMed Scopus Google Scholar) or S. J. Biol. Chem. 1998; Full Text Full Text PDF PubMed Scopus Google Scholar). or of a by and a for or an and an A. J. Biol. Chem. 1997; 272: Full Text Full Text PDF PubMed Scopus Google Scholar). The in the by a which binds C. K. Biochem. PubMed Scopus Google Scholar). The of by The as the of the of to the of and by the of the by as described K. H. 1991; PubMed Scopus Google Scholar), and with The signals a The a a CYH2 a an and an from the and by K. a novel that the general translation machinery, we the of environmental stresses on protein synthesis by in the of methionine uptake by a to and by with and it not to the the the uptake of in the in an of cells this in uptake than a in protein synthesis stress. For this we used the of to in as the of protein The of methionine from the to the A and which is with has been reported (9.Varela J.C. van Beekvelt C. Planta R.J. Mager W.H. Mol. Microbiol. 1992; 6: 2183-2190Crossref PubMed Scopus (92) Google Scholar). of that the of protein synthesis after to the stress and to the protein synthesis not after to heat stress or stress. the stresses than other stresses in an on protein We examined the effect of on methionine uptake and protein The of methionine uptake as the of and not to the that inhibits the uptake of methionine In the to after and to the that the inhibition of uracil uptake by is the of protein synthesis also rapidly but to of the of methionine uptake stress and not the inhibition of amino acid uptake by stress in the inhibition of protein synthesis but not in (9.Varela J.C. van Beekvelt C. Planta R.J. Mager W.H. Mol. Microbiol. 1992; 6: 2183-2190Crossref PubMed Scopus (92) Google Scholar) also reported a in methionine uptake by osmotic stress such as However, reported that the inhibition results that the inhibition of methionine uptake by osmotic stress such as or is we examined the of the and Hog1 in the inhibition of nutrient uptake and protein The of methionine uptake in both and the after and not to the results in the In to the of the of glucose uptake in the after in the These results that stress inhibits the uptake of methionine of the Hog1 MAPK pathway, it the uptake of glucose in a Hog1 MAP The of protein synthesis after but to the in the after in the of This of protein synthesis after inhibition by synthesis in the as it in the after but the of protein synthesis in both to of that in These results that the Hog1 MAPK pathway is not involved in the inhibition of protein synthesis but to stimulate the of protein synthesis after it is we examined the Hog1 MAPK pathway stimulate protein synthesis in the of stress. The an in the of protein synthesis in with cells This result that the Hog1 MAPK pathway not protein synthesis but is involved in the adaptation of protein synthesis after the the initiation or the of we cells to osmotic to the to translation and the of of carried in the after to the stress as the of The that the effect of than that of be of the of cells to as described and the of the has been in in translation initiation L. H. J. H. J. Biol. Chem. 1998; Full Text Full Text PDF PubMed Scopus Google Scholar, A. EMBO J. 1999; PubMed Scopus (92) Google Scholar, U. S. A. 62: PubMed Scopus Google Scholar), results that the inhibits the initiation of also translation initiation that the inhibition is to the osmotic stress and is not specific to we examined the of the changes in the after the of cells to a of the a and to the The of the of cells with a and to the Thus, we that osmotic stress inhibits translation initiation. the to or the as in cells but not to the and The a result to the not These that the Hog1 MAPK pathway is not involved in translation inhibition but is required for adaptation of translation initiation after In the of with the of inhibition by the of that by This is of the different used for the used for the of and used for is also that the adaptation in the is a effect from the inhibition of the glucose-sensing pathway that translation initiation, as described in The uptake of glucose in the that in the after However, the of cells not as the the glucose in the from to the in adaptation of translation initiation in the is not to a in glucose the of the transient inhibition the in to the of and and mRNAs The of and not after in either the or the The in and after and These results suggest that osmotic stress not the of the cell translation the and the initiation and the after osmotic in the but not in in This that the initiation is the adaptation to osmotic stress and that Hog1 MAP kinase also be required for of the initiation the adaptation of amino acids or glucose from the and rapamycin are known to the inhibition of translational initiation (1.McCarthy J.E.G. Microbiol. Mol. Biol. Rev. 1998; 62: 1492-1553Crossref PubMed Google Scholar, 4.Ashe M.P. De Long S.K. Sachs A.B. Mol. Biol. Cell. 2000; 11: 833-848Crossref PubMed Scopus (314) Google Scholar). osmotic stress inhibits translation initiation through we examined in osmotic stress the uptake of as described in it is that amino acid inhibits translation initiation as a effect of the osmotic stress. this we used the which has the of to in the α-subunit of eIF2, translation initiation to the inhibition by the deprivation of amino the to or to a glucose for the inhibition of translational initiation to the as in the the translation initiation not the to amino acids (4.Ashe M.P. De Long S.K. Sachs A.B. Mol. Biol. Cell. 2000; 11: 833-848Crossref PubMed Scopus (314) Google Scholar). This that the inhibition of translation by osmotic stress occurs through a other than the phosphorylation of the osmotic stress the translation initiation in a cell that not amino acid a to that the inhibition of translation by osmotic stress occurs through a different pathway than amino acid However, the inhibition in the cell with than in the cell that the inhibition of translation initiation by osmotic stress in on the amino acid by osmotic stress. The is known to be a of the M.P. C. Mol. Cell. Biol. 1995; PubMed Scopus Google Scholar) and to be involved in poly(A) M. J. R. Cell. 2001; Full Text Full Text PDF PubMed Scopus Google Scholar) and the glucose pathway A. F. 1992; PubMed Scopus Google Scholar). Recently, H. A. S. M. A. 2001; PubMed Scopus Google Scholar) reported that is rapidly glucose the of the phosphorylation to that of the translation inhibition glucose we examined is involved in the translation inhibition glucose in deprivation of glucose for not inhibit the translation initiation in the that to the translation inhibition the of glucose as in the of the or which are also involved in the glucose-sensing pathway (4.Ashe M.P. De Long S.K. Sachs A.B. Mol. Biol. Cell. 2000; 11: 833-848Crossref PubMed Scopus (314) Google Scholar). However, the of glucose deprivation used in this the translation initiation in not that the has a than in the inhibition of translation glucose In osmotic stress inhibit translation initiation in the to the as in the In osmotic stress also initiation in which has a of the protein kinase A activity that is required for glucose deprivation of glucose or amino acids not inhibit initiation in as reported (4.Ashe M.P. De Long S.K. Sachs A.B. Mol. Biol. Cell. 2000; 11: 833-848Crossref PubMed Scopus (314) Google Scholar). The inhibition of translation by stresses in the for the and for as the for the not These results also suggest that the inhibition of translation by osmotic stress is by a different from that by glucose or amino acid the of inhibition of translation initiation by osmotic stress in the than that in the it is that osmotic translation inhibition not the protein kinase A activity effect of the protein kinase A we used the A. M.P. S. EMBO J. 1998; PubMed Scopus Google Scholar). Translation inhibition by osmotic stress in the to the it in the Translation inhibition by deprivation of amino acids or glucose also to as reported (4.Ashe M.P. De Long S.K. Sachs A.B. Mol. Biol. Cell. 2000; 11: 833-848Crossref PubMed Scopus (314) Google Scholar). Thus, the of to inhibit translation on the expression by than on protein kinase A activity the translation initiation of the rapamycin the growth of on not This inhibition of translation initiation by rapamycin with (6.Barbet N.C. Schneider U. Helliwell S.B. Stansfield I. Tuite M.F. Hall M.N. Mol. Biol. Cell. 1996; 7: 25-42Crossref PubMed Scopus (603) Google Scholar, P. Mol. Biol. Cell. 1999; PubMed Scopus Google Scholar). We also found that the to the to rapamycin it is that the of the cell is required for to the to the or not This is with the that rapamycin inhibits via the pathway A. A. Kunz J. Hall M.N. EMBO J. 1998; PubMed Scopus Google Scholar). However, the to rapamycin not that are specific to the stress the translation initiation in the in which translation is to rapamycin These results suggest that the inhibition of translation initiation by osmotic stress not result from of the pathway. stress causes transient repression of many including RP genes W.H. J.C. Mol. Microbiol. PubMed Scopus (92) Google Scholar, 13.Gasch A.P. Spellman P.T. Kao C.M. Carmel-Harel O. Eisen M.B. Gisela S. Botstein D. Brown P.O. Mol. Biol. Cell. 2000; 11: 4241-4257Crossref PubMed Scopus (3762) Google Scholar). Thus, it is that the inhibition of translational initiation by osmotic stress occurs as a result of the inhibition of than the effect of expression on translation inhibition by osmotic we examined the expression of the RP genes as an of osmotic In cells the of mRNA of CYH2 or to after with mRNA and to the by with the of both the of the RP mRNAs and the of mRNA to in the These results that osmotic stress causes a transient of the RP described the of translational inhibition of the with and and that the translation inhibition the of the RP In the translation initiation to in the cells with the RP mRNAs not These results that the translation inhibition not with the of the RP the with or the of the RP mRNAs and of the mRNA not A and In the expression the of to of that in cells This that the Hog1 MAPK pathway to the transient of the RP mRNA as as to the of many including in to osmotic stress (12.Posas F. Chambers J.R. Heyman J.A. Hoeffler J.P. de Nadal E. Arino J. J. Biol. Chem. 2000; 275: 17249-17255Abstract Full Text Full Text PDF PubMed Scopus (335) Google Scholar). The translation inhibition of the by osmotic stress an of the RP or mRNAs These results also suggest that the translation inhibition by osmotic stress is a than a effect of the of expression by osmotic stress. the of the in the of for to after a to a that to of mRNA synthesis not (4.Ashe M.P. De Long S.K. Sachs A.B. Mol. Biol. Cell. 2000; 11: 833-848Crossref PubMed Scopus (314) Google Scholar), as in the of cells or the (6.Barbet N.C. Schneider U. Helliwell S.B. Stansfield I. Tuite M.F. Hall M.N. Mol. Biol. Cell. 1996; 7: 25-42Crossref PubMed Scopus (603) Google Scholar, P. Mol. Biol. Cell. 1999; PubMed Scopus Google Scholar). This than that of the osmotic inhibition of translation initiation. it is not that the of the in to osmotic stress is to repression of the expression of many In rapamycin of yeast cells causes repression of the RP genes the inhibition of translation initiation (6.Barbet N.C. Schneider U. Helliwell S.B. Stansfield I. Tuite M.F. Hall M.N. Mol. Biol. Cell. 1996; 7: 25-42Crossref PubMed Scopus (603) Google Scholar, P. Mol. Biol. Cell. 1999; PubMed Scopus Google Scholar). These also suggest that translational inhibition by osmotic stress be by a distinct from that of rapamycin cerevisiae, the translation initiation factor by the genes has been to as an a poly(A) and a factor A.B. P. Cell. 1997; Full Text Full Text PDF PubMed Scopus Google Scholar). The protein has been reported to be the of rapamycin or nutrient deprivation C. H. M. U. S. A. 1998; PubMed Scopus Google Scholar). However, changes in the of and a yeast of M. S. R. R. EMBO J. 1998; PubMed Scopus Google Scholar), after of the that rapamycin causes and inhibition of translation initiation as with osmotic that osmotic stress inhibit translation initiation in cells and that osmotic stress inhibit the translation initiation the repression of the RP genes also that osmotic stress inhibits the translation initiation by a other than the TOR pathway. We the by (9.Varela J.C. van Beekvelt C. Planta R.J. Mager W.H. Mol. Microbiol. 1992; 6: 2183-2190Crossref PubMed Scopus (92) Google Scholar) that osmotic stress causes the inhibition of methionine uptake and found that the Hog1 MAP kinase pathway is not required for this we that are nutrient uptake osmotic stress to transient inhibition of uracil uptake, transient stimulation of glucose uptake, and irreversible inhibition of methionine uptake The growth of yeast cells is in to an in external osmolarity J. A. J. Biol. Chem. 1997; 272: Full Text Full Text PDF PubMed Scopus Google Scholar). This to the irreversible of methionine the uptake of nutrients for growth be an in the The uptake inhibition result in the of growth of an of nutrients for cell of a number of genes is or in to osmotic stress. The Hog1 pathway and factors are known to function in the transient (12.Posas F. Chambers J.R. Heyman J.A. Hoeffler J.P. de Nadal E. Arino J. J. Biol. Chem. 2000; 275: 17249-17255Abstract Full Text Full Text PDF PubMed Scopus (335) Google Scholar, 14.Causton H.C. Ren B. Koh S.S. Harbison C.T. Kanin E. Jennings E.G. Lee T.I. True H.L. Lander E.S. Young R.A. Mol. Biol. Cell. 2001; 12: 323-337Crossref PubMed Scopus (1077) Google Scholar, C. H. EMBO J. 1994; PubMed Scopus Google Scholar). However, been the factors involved in the transient of expression by osmotic stress. is the that the Hog1 pathway is required for the transient of expression of genes such as the RP genes that osmotic stress causes the transient inhibition of protein synthesis with (9.Varela J.C. van Beekvelt C. Planta R.J. Mager W.H. Mol. Microbiol. 1992; 6: 2183-2190Crossref PubMed Scopus (92) Google Scholar). However, it not known osmotic stress inhibits the initiation or the of In this study, that the inhibition by osmotic stress is the initiation In results that the Hog1 MAP kinase pathway is not required for the inhibition of translation initiation but is required for adaptation of the translation initiation after osmotic In of translation initiation, the to osmotic stress are the inhibition by an and the activation that be by the Hog1 MAPK pathway the adaptation of translation initiation Thus, it is to the of transient inhibition as The inhibition after as in the phosphorylation of Hog1 occurs and after with and de E. Science. PubMed Scopus Google Scholar, I. 1998; 12: PubMed Scopus Google Scholar), the Hog1 MAPK pathway is the inhibition of translation by the of cells with the The activation of translation for a through the expression by the Hog1 MAPK pathway, the inhibition for a a result of a combination of both the of inhibition and the long-term of the translation is after the osmotic inhibition of translation initiation and or after the of the expression of the in the A and not in the that is in the expression of genes A and These results the that the adaptation of translation occurs as a result of expression by the Hog1 MAPK pathway. However, protein synthesis and to and after the of the transient expression of many including F. Chambers J.R. Heyman J.A. Hoeffler J.P. de Nadal E. Arino J. J. Biol. Chem. 2000; 275: 17249-17255Abstract Full Text Full Text PDF PubMed Scopus (335) Google Scholar), that the adaptation of translation not on the transient expression of the Hog1 MAPK We that the Hog1 MAPK pathway also to the adaptation of translation as as to of yeast cells to osmotic causes a in cell after which the cells has been that the in cell growth is of a transient of or S. J. Biol. 1992; PubMed Scopus Google Scholar, I. S. A. Microbiol. 2000; PubMed Scopus Google Scholar). The of the transient of to osmotic stress that of the transient inhibition of translation initiation by osmotic that the transient inhibition of translation initiation also be a to the in growth after osmotic stress. is the of the transient inhibition of translation has been reported that the of is by osmotic stress J. A. J. Biol. Chem. 1997; 272: Full Text Full Text PDF PubMed Scopus Google Scholar). of the is that of translation initiation but not increases which are not by be by the cells the of mRNAs by changes in or regulation of mRNAs the the cell the to the of mRNAs by the translation is that the cell the of in to an environmental We M. A. B. A. J. A. M. D. S. and M. for and and for as as the of