Viral IRES RNA structures and ribosome interactions

by: Jeffrey S Kieft

Trends in Biochemical Sciences, Vol. 33, No. 6. (June 2008), pp. 274-283.

View FullText article

DOI, ScienceDirect

Reviews [Write a review of this article]

There are no reviews of this article

Find related articles from these CiteULike users

wsjames, Oxford Virology (group)

Find related articles with these CiteULike tags

replication, structure

摘要

In eukaryotes, protein synthesis initiates primarily by a mechanism that requires a modified nucleotide [`]cap' on the mRNA and also proteins that recruit and position the ribosome. Many pathogenic viruses use an alternative, cap-independent mechanism that substitutes RNA structure for the cap and many proteins. The RNAs driving this process are called internal ribosome-entry sites (IRESs) and some are able to bind the ribosome directly using a specific 3D RNA structure. Recent structures of IRES RNAs and IRES-ribosome complexes are revealing the structural basis of viral IRES' [`]hijacking' of the protein-making machinery. It now seems that there are fundamental differences in the 3D structures used by different IRESs, although there are some common features in how they interact with ribosomes.

@article{citeulike:2889643, abstract = {In eukaryotes, protein synthesis initiates primarily by a mechanism that requires a modified nucleotide [`]cap' on the mRNA and also proteins that recruit and position the ribosome. Many pathogenic viruses use an alternative, cap-independent mechanism that substitutes RNA structure for the cap and many proteins. The RNAs driving this process are called internal ribosome-entry sites (IRESs) and some are able to bind the ribosome directly using a specific 3D RNA structure. Recent structures of IRES RNAs and IRES-ribosome complexes are revealing the structural basis of viral IRES' [`]hijacking' of the protein-making machinery. It now seems that there are fundamental differences in the 3D structures used by different IRESs, although there are some common features in how they interact with ribosomes.}, author = {Kieft, Jeffrey S. }, citeulike-article-id = {2889643}, doi = {http://dx.doi.org/10.1016/j.tibs.2008.04.007}, journal = {Trends in Biochemical Sciences}, keywords = {replication, structure}, month = {June}, number = {6}, pages = {274--283}, posted-at = {2008-06-12 17:26:49}, priority = {2}, title = {Viral IRES RNA structures and ribosome interactions}, url = {http://dx.doi.org/10.1016/j.tibs.2008.04.007}, volume = {33}, year = {2008} }

RIS record

TY - JOUR ID - citeulike:2889643 L3 - citeulike-article-id:2889643 N2 - In eukaryotes, protein synthesis initiates primarily by a mechanism that requires a modified nucleotide [`]cap' on the mRNA and also proteins that recruit and position the ribosome. Many pathogenic viruses use an alternative, cap-independent mechanism that substitutes RNA structure for the cap and many proteins. The RNAs driving this process are called internal ribosome-entry sites (IRESs) and some are able to bind the ribosome directly using a specific 3D RNA structure. Recent structures of IRES RNAs and IRES-ribosome complexes are revealing the structural basis of viral IRES' [`]hijacking' of the protein-making machinery. It now seems that there are fundamental differences in the 3D structures used by different IRESs, although there are some common features in how they interact with ribosomes. IS - 6 JF - Trends in Biochemical Sciences EP - 283 TI - Viral IRES RNA structures and ribosome interactions VL - 33 SP - 274 KW - replication KW - structure AU - Kieft, Jeffrey PY - 2008/06// UR - http://dx.doi.org/10.1016/j.tibs.2008.04.007 ER -

RIS BibTeX