Getting to the end of RNA: Structural analysis of protein recognition of 5′ and 3′ termini

The specific recognition by proteins of the 5′ and 3′ ends of RNA molecules is an important facet of many cellular processes, including RNA maturation, regulation of translation initiation and control of gene expression by degradation and RNA interference. The aim of this review is to survey recent...

Full description

Saved in:
Bibliographic Details
Published inBiochimica et biophysica acta Vol. 1789; no. 9; pp. 653 - 666
Main Authors Curry, Stephen, Kotik-Kogan, Olga, Conte, Maria R., Brick, Peter
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 01.09.2009
Subjects
Online AccessGet full text

Cover

Loading…
More Information
Summary:The specific recognition by proteins of the 5′ and 3′ ends of RNA molecules is an important facet of many cellular processes, including RNA maturation, regulation of translation initiation and control of gene expression by degradation and RNA interference. The aim of this review is to survey recent structural analyses of protein binding domains that specifically bind to the extreme 5′ or 3′ termini of RNA. For reasons of space and because their interactions are also governed by catalytic considerations, we have excluded enzymes that modify the 5′ and 3′ extremities of RNA. It is clear that there is enormous structural diversity among the proteins that have evolved to bind to the ends of RNA molecules. Moreover, they commonly exhibit conformational flexibility that appears to be important for binding and regulation of the interaction. This flexibility has sometimes complicated the interpretation of structural results and presents significant challenges for future investigations.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-3
content type line 23
ObjectType-Review-1
ObjectType-Feature-1
ISSN:1874-9399
0006-3002
1876-4320
DOI:10.1016/j.bbagrm.2009.07.003