Protein Science · 2016 · 13 citations · 62 references
Life SciencesGeneticsMolecular BiologyRna ProcessingTranscriptionTranscriptional RegulationRna-binding ProteinsRna-protein InteractionsTranscription ElongationTranscription In EukaryotesCo-transcriptional Mrna ProcessingCo-transcriptional Rna ProcessingRna Recognition MotifsRna-protein RecognitionSequence-specific RecognitionTranscription Elongation ComplexesTranscription Elongation ControlTranscriptional Elongation Control
The heterodimeric transcription elongation factor Spt4/Spt5 (Spt4/5) tightly associates with RNAPII to regulate both transcriptional elongation and co-transcriptional pre-mRNA processing; however, the mechanisms by which Spt4/5 acts are poorly understood. Recent studies of the human and Drosophila Spt4/5 complexes indicate that they can bind nucleic acids in vitro. We demonstrate here that yeast Spt4/5 can bind in a sequence-specific manner to single stranded RNA containing AAN repeats. Furthermore, we show that the major protein determinants for RNA-binding are Spt4 together with the NGN domain of Spt5 and that the KOW domains are not required for RNA recognition. These findings attribute a new function to a domain of Spt4/5 that associates directly with RNAPII, making significant steps towards elucidating the mechanism behind transcriptional control by Spt4/5.
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The PyMOL Molecular Graphics System
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M. Selmer, C.M. Dunham, F.V. Murphy et al. · Science · 2006 · 1.3K citations
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Rahul C. Deo, J.B. Bonanno, Nahum Sonenberg et al. · Cell · 1999 · 517 citations · Full text