Journal of Biological Chemistry · 1981 · 78 citations · 23 references
Life SciencesBiochemistryMolecular BiologyChromatin BiologyChromatin StructureAmino Acid Sequence DeterminantsChromatinHistone ProteinsNucleosome StructureProtein Sequence AnalysisProtein StructureDna Binding Protein MotifsHistone Core StructureHistone-dna Interactions
The complete amino acid sequence of the DNA-binding histone-like protein (Hta) from Thermoplasma acidophilum has been established by sequence studies directly on the protein and on tryptic, chymotryptic, and thermolysin peptides derived from the protein. The sequence of the 89-residue form of HTa is: H2N-Val-Gly-Ile-Ser-Glu-Leu-Ser-Lys-Glu-Val-Ala-Lys-Lys-Ala-Asn-Thr-Thr-Gln-Lys -Val-Ala-Arg-Thr-Val-Ile-Lys-Ser-Phe-Leu-Asp-Glu-Ile-Val-Ser-Glu-Ala-Asn-Gly-Gl y-Gln-Lys-Ile-Asn-Leu-Ala-Gly-Phe-Gly-Ile-Phe-Glu-Arg-Arg-Thr-Gln-Gly-Pro-Arg-L ys-Ala-Arg-Asn-Pro-Gln-Thr-Lys-Lys-Val-Ile-Glu-Val-Pro-Ser-Lys-Lys-Lys-Phe-Val- Phe-Arg-Ala-Ser-Ser-Lys-Ile-Lys-Tyr-Gln-Gln-COOH The molecular weight calculated from the sequence is 9,934. Another form of HTa probably differs only by the presence of an additional residue (methionine) at the NH2 terminus (the calculated molecular weight of this form is 10,065). HTa resembles eukaryotic histones in several ways, including some sequence homology, HTa also shows sequence homology with the Escherichia coli DNA-binding proteins NS1 (or HU-1) and NS2 (or HU-2).
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Soybeans: Improvement, production, and uses
J. S. Russell · Field Crops Research · 1988 · 794 citations
Agriculture, Agronomy, Crop Sciences +10
Subunit Structure of Soybean Agglutinin
Reuben Lotan, H. W. Siegelman, Halina Lis et al. · Journal of Biological Chemistry · 1974 · 209 citations · Full text