2KM4
Solution structure of Rtt103 CTD interacting domain
Summary for 2KM4
| Entry DOI | 10.2210/pdb2km4/pdb |
| NMR Information | BMRB: 16411 |
| Descriptor | Regulator of Ty1 transposition protein 103 (1 entity in total) |
| Functional Keywords | ctd-interacting domain, rna polymerase ii binding protein, phosphoprotein, transcription termination, dna-binding, nucleus, transcription, transcription regulation, transcription regulator |
| Biological source | Saccharomyces cerevisiae (yeast) |
| Cellular location | Nucleus: Q05543 |
| Total number of polymer chains | 1 |
| Total formula weight | 16569.10 |
| Authors | Lunde, B.M.,Reichow, S.,Kim, M.,Leeper, T.C.,Becker, R.,Buratowski, S.,Meinhart, A.,Varani, G. (deposition date: 2009-07-20, release date: 2010-09-08, Last modification date: 2024-05-01) |
| Primary citation | Lunde, B.M.,Reichow, S.L.,Kim, M.,Suh, H.,Leeper, T.C.,Yang, F.,Mutschler, H.,Buratowski, S.,Meinhart, A.,Varani, G. Cooperative interaction of transcription termination factors with the RNA polymerase II C-terminal domain. Nat.Struct.Mol.Biol., 17:1195-1201, 2010 Cited by PubMed Abstract: Phosphorylation of the C-terminal domain (CTD) of RNA polymerase II controls the co-transcriptional assembly of RNA processing and transcription factors. Recruitment relies on conserved CTD-interacting domains (CIDs) that recognize different CTD phosphoisoforms during the transcription cycle, but the molecular basis for their specificity remains unclear. We show that the CIDs of two transcription termination factors, Rtt103 and Pcf11, achieve high affinity and specificity both by specifically recognizing the phosphorylated CTD and by cooperatively binding to neighboring CTD repeats. Single-residue mutations at the protein-protein interface abolish cooperativity and affect recruitment at the 3' end processing site in vivo. We suggest that this cooperativity provides a signal-response mechanism to ensure that its action is confined only to proper polyadenylation sites where Ser2 phosphorylation density is highest. PubMed: 20818393DOI: 10.1038/nsmb.1893 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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