RNA-BINDING DOMAIN OF THE A-PROTEIN COMPONENT OF THE U1 SMALL NUCLEAR RIBONUCLEOPROTEIN ANALYZED BY NMR-SPECTROSCOPY IS STRUCTURALLY SIMILAR TO RIBOSOMAL-PROTEINS

被引：198

作者：

HOFFMAN, DW ^{[1
]}

QUERY, CC ^{[1
]}

GOLDEN, BL ^{[1
]}

WHITE, SW ^{[1
]}

KEENE, JD ^{[1
]}

机构：

[1] DUKE UNIV, MED CTR, DEPT MICROBIOL & IMMUNOL, DURHAM, NC 27710 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1991年 / 88卷 / 06期

关键词：

NMR STRUCTURE; RIBONUCLEOPROTEIN CONSENSUS SEQUENCE; RNA RECOGNITION MOTIF;

D O I：

10.1073/pnas.88.6.2495

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

An RNA recognition motif (RRM) of almost-equal-to 80 amino acids constitutes the core of RNA-binding domains found in a large family of proteins involved in RNA processing. The U1 RNA-binding domain of the A protein component of the human U1 small nuclear ribonucleoprotein (RNP), which encompasses the RRM sequence, was analyzed by using NMR spectroscopy. The domain of the A protein is a highly stable monomer in solution consisting of four antiparallel beta-strands and two alpha-helices. The highly conserved RNP1 and RNP2 consensus sequences, containing residues previously suggested to be involved in nucleic acid binding, are juxtaposed in adjacent beta-strands. Conserved aromatic side chains that are critical for RNA binding are clustered on the surface of the molecule adjacent to a variable loop that influences recognition of specific RNA sequences. The secondary structure and topology of the RRM are similar to those of ribosomal proteins L12 and L30, suggesting a distant evolutionary relationship between these two types of RNA-associated proteins.

引用

页码：2495 / 2499

页数：5