3NYB

Structure and function of the polymerase core of TRAMP, a RNA surveillance complex

3NYB の概要

• エントリーDOI: 10.2210/pdb3nyb/pdb
• 分子名称: Poly(A) RNA polymerase protein 2, Protein AIR2, ZINC ION, ... (4 entities in total)
• 機能のキーワード: polya rna polymerase, zinc knuckle protein, rna surveillance, mtr4p binds to trf4p/air2p heterodimer, transferase-rna binding protein complex, transferase/rna binding protein
• 由来する生物種: Saccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 45990.03

構造登録者

Reinisch, K.M.,Hamill, S. (登録日: 2010-07-14, 公開日: 2010-08-04, 最終更新日: 2024-02-21)

主引用文献

Hamill, S.,Wolin, S.L.,Reinisch, K.M.
Structure and function of the polymerase core of TRAMP, a RNA surveillance complex.
Proc.Natl.Acad.Sci.USA, 107:15045-15050, 2010

PubMed Abstract: The Trf4p/Air2p/Mtr4p polyadenylation (TRAMP) complex recognizes aberrant RNAs in Saccharomyces cerevisiae and targets them for degradation. A TRAMP subcomplex consisting of a noncanonical poly(A) RNA polymerase in the Pol ss superfamily of nucleotidyl transferases, Trf4p, and a zinc knuckle protein, Air2p, mediates initial substrate recognition. Trf4p and related eukaryotic poly(A) and poly(U) polymerases differ from other characterized enzymes in the Pol ss superfamily both in sequence and in the lack of recognizable nucleic acid binding motifs. Here we report, at 2.7-A resolution, the structure of Trf4p in complex with a fragment of Air2p comprising two zinc knuckle motifs. Trf4p consists of a catalytic and central domain similar in fold to those of other noncanonical Pol beta RNA polymerases, and the two zinc knuckle motifs of Air2p interact with the Trf4p central domain. The interaction surface on Trf4p is highly conserved across eukaryotes, providing evidence that the Trf4p/Air2p complex is conserved in higher eukaryotes as well as in yeast and that the TRAMP complex may also function in RNA surveillance in higher eukaryotes. We show that Air2p, and in particular sequences encompassing a zinc knuckle motif near its N terminus, modulate Trf4p activity, and we present data supporting a role for this zinc knuckle in RNA binding. Finally, we show that the RNA 3' end plays a role in substrate recognition.

PubMed: 20696927
DOI: 10.1073/pnas.1003505107

実験手法

X-RAY DIFFRACTION (2.7007 Å)