3D9L

Snapshots of the RNA processing factor SCAF8 bound to different phosphorylated forms of the Carboxy-Terminal Domain of RNA-Polymerase II

Summary for 3D9L

• Entry DOI: 10.2210/pdb3d9l/pdb
• Related: 1sz9 1sza 2bf0 3D9I 3D9J 3D9K 3D9M 3D9N 3D9O 3D9P 3clj
• Descriptor: RNA-binding protein 16, CTD-PEPTIDE, ACETATE ION, ... (5 entities in total)
• Functional Keywords: scaf8, rna polymerase ii ctd interacting domain, arm repeats, phospho-ctd, phosphoprotein, rna-binding, transcription-peptide complex, transcription/peptide
• Biological source: Homo sapiens (man); More
• Cellular location: Nucleus: Q9UPN6
• Total number of polymer chains: 4
• Total formula weight: 37719.93

Authors

Becker, R.,Loll, B.,Meinhart, A. (deposition date: 2008-05-27, release date: 2008-06-10, Last modification date: 2023-08-30)

Primary citation

Becker, R.,Loll, B.,Meinhart, A.
Snapshots of the RNA Processing Factor SCAF8 Bound to Different Phosphorylated Forms of the Carboxyl-terminal Domain of RNA Polymerase II.
J.Biol.Chem., 283:22659-22669, 2008

PubMed Abstract: Concomitant with RNA polymerase II (Pol II) transcription, RNA maturation factors are recruited to the carboxyl-terminal domain (CTD) of Pol II, whose phosphorylation state changes during a transcription cycle. CTD phosphorylation triggers recruitment of functionally different factors involved in RNA processing and transcription termination; most of these factors harbor a conserved CTD interacting domain (CID). Orchestration of factor recruitment is believed to be conducted by CID recognition of distinct phosphorylated forms of the CTD. We show that the human RNA processing factor SCAF8 interacts weakly with the unphosphorylated CTD of Pol II. Upon phosphorylation, affinity for the CTD is increased; however, SCAF8 is promiscuous to the phosphorylation pattern on the CTD. Employing a combined structural and biophysical approach, we were able to distinguish motifs within CIDs that are involved in a generic CTD sequence recognition from items that confer phospho-specificity.

PubMed: 18550522
DOI: 10.1074/jbc.M803540200

Experimental method

X-RAY DIFFRACTION (2.2 Å)