RNA recognition by the Vts1p SAM domain

被引：54
|
作者：
Johnson, PE
Donaldson, LW
机构：
[1] York Univ, Dept Chem, N York, ON M3J 1P3, Canada
[2] York Univ, Dept Biol, N York, ON M3J 1P3, Canada
来源：
NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2006年 / 13卷 / 02期
基金：
加拿大健康研究院;
关键词：
D O I：
10.1038/nsmb1039
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The putative yeast post-transcriptional regulator Vts1p and its related protein Smaug, from Drosophila melanogaster, each use a sterile alpha motif (SAM) domain to bind an RNA hairpin termed the Smaug recognition element (SRE). Here, we present the NMR structures of the Vts1p - SRE complex and the free SRE. Structural highlights include the direct recognition of a guanine base and the formation or stabilization of a base pair in the SRE loop.
引用
收藏
页码：177 / 178
页数：2
相关论文
共 50 条
  • [41] The RNA-binding SAM domain of Smaug defines a new family of post-transcriptional regulators
    Aviv, T
    Lin, Z
    Lau, S
    Rendl, LM
    Sicheri, F
    Smibert, CA
    NATURE STRUCTURAL BIOLOGY, 2003, 10 (08) : 614 - 621
  • [42] Structural basis for the recognition of RNA polymerase II C-terminal domain by CREPT and p15RS
    KunRong Mei
    Zhe Jin
    FangLi Ren
    YinYing Wang
    ZhiJie Chang
    XinQuan Wang
    Science China Life Sciences, 2014, 57 : 97 - 106
  • [43] Electroretinogram (ERG) analysis in senescence-accelerated mouse (SAM) strains SAM R1 and SAM P8
    Zangemeister, AC
    Brandeweide, J
    Morellini, F
    Richard, G
    Reuther, K
    INVESTIGATIVE OPHTHALMOLOGY & VISUAL SCIENCE, 2002, 43 : U982 - U982
  • [44] The RNA-binding SAM domain of Smaug defines a new family of post-transcriptional regulators
    Tzvi Aviv
    Zhen Lin
    Stefanie Lau
    Laura M. Rendl
    Frank Sicheri
    Craig A Smibert
    Nature Structural & Molecular Biology, 2003, 10 : 614 - 621
  • [45] p53 Family members p63 and p73 are SAM domain-containing proteins
    Thanos, CD
    Bowie, JU
    PROTEIN SCIENCE, 1999, 8 (08) : 1708 - 1710
  • [46] RNA Ensembles from Solvent Accessibility Data: Application to the SAM-I Riboswitch Aptamer Domain
    Xie, Jingru
    Frank, Aaron T.
    JOURNAL OF PHYSICAL CHEMISTRY B, 2021, 125 (14): : 3486 - 3493
  • [47] Structural basis of RNA recognition and dimerization by the STAR proteins T-STAR and Sam68
    Mikael Feracci
    Jaelle N. Foot
    Sushma N. Grellscheid
    Marina Danilenko
    Ralf Stehle
    Oksana Gonchar
    Hyun-Seo Kang
    Caroline Dalgliesh
    N. Helge Meyer
    Yilei Liu
    Albert Lahat
    Michael Sattler
    Ian C. Eperon
    David J. Elliott
    Cyril Dominguez
    Nature Communications, 7
  • [48] Structural basis of RNA recognition and dimerization by the STAR proteins T-STAR and Sam68
    Feracci, Mikael
    Foot, Jaelle N.
    Grellscheid, Sushma N.
    Danilenko, Marina
    Stehle, Ralf
    Gonchar, Oksana
    Kang, Hyun-Seo
    Dalgliesh, Caroline
    Meyer, N. Helge
    Liu, Yilei
    Lahat, Albert
    Sattler, Michael
    Eperon, Ian C.
    Elliott, David J.
    Dominguez, Cyril
    NATURE COMMUNICATIONS, 2016, 7
  • [49] Recognition of Archaeal CRISPR RNA: No P in the alindromic Repeat?
    Lawrence, C. Martin
    White, Malcolm F.
    STRUCTURE, 2011, 19 (02) : 142 - 144
  • [50] The SAM domain of mouse SAMHD1 is critical for its activation and regulation
    Buzovetsky, Olga
    Tang, Chenxiang
    Knecht, Kirsten M.
    Antonucci, Jenna M.
    Wu, Li
    Ji, Xiaoyun
    Xiong, Yong
    NATURE COMMUNICATIONS, 2018, 9
12345