Ro's role in RNA reconnaissance

Ian J MacRae; Jennifer A Doudna

doi:10.1016/j.cell.2005.05.004

Ro's role in RNA reconnaissance

Cell. 2005 May 20;121(4):495-496. doi: 10.1016/j.cell.2005.05.004.

Authors

Ian J MacRae¹, Jennifer A Doudna²

Affiliations

¹ Howard Hughes Medical Institute, Department of Molecular & Cell Biology and Department of Chemistry, Lawrence Berkeley National Laboratory, University of California at Berkeley, Berkeley, California 94720; Physical Biosciences Division, Lawrence Berkeley National Laboratory, University of California at Berkeley, Berkeley, California 94720.
² Howard Hughes Medical Institute, Department of Molecular & Cell Biology and Department of Chemistry, Lawrence Berkeley National Laboratory, University of California at Berkeley, Berkeley, California 94720; Physical Biosciences Division, Lawrence Berkeley National Laboratory, University of California at Berkeley, Berkeley, California 94720. Electronic address: doudna@uclink.berkeley.edu.

PMID: 15907458
DOI: 10.1016/j.cell.2005.05.004

Abstract

The Ro 60 kDa autoantigen binds misfolded RNAs and likely functions in small RNA quality control. In this issue of Cell, Stein et al. (2005) present crystal structures of Ro alone and bound to both double- and single-stranded RNA, revealing two distinct RNA binding sites that suggest how Ro may distinguish between native and misfolded small RNAs.

Publication types

Comment
Review

MeSH terms

Animals
Binding Sites / physiology
Humans
Protein Structure, Tertiary / physiology
RNA / genetics
RNA / metabolism*
RNA, Small Cytoplasmic / genetics
RNA, Small Cytoplasmic / metabolism
RNA, Small Nuclear / genetics
RNA, Small Nuclear / metabolism
RNA-Binding Proteins / genetics
RNA-Binding Proteins / metabolism*
Ribonucleoproteins / chemistry*
Ribonucleoproteins / genetics
Ribonucleoproteins / metabolism*

Substances

RNA, Small Cytoplasmic
RNA, Small Nuclear
RNA-Binding Proteins
Ribonucleoproteins
SS-A antigen
RNA