3′ Cap-Independent Translation Enhancers of Plant Viruses

Simon, Anne E.; Miller, W. Allen

doi:10.1146/annurev-micro-092412-155609

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CDC STACKS serves as an archival repository of CDC-published products including scientific findings, journal articles, guidelines, recommendations, or other public health information authored or co-authored by CDC or funded partners. As a repository, CDC STACKS retains documents in their original published format to ensure public access to scientific information.

i

3′ Cap-Independent Translation Enhancers of Plant Viruses

May 13 2013
By Simon, Anne E. ; Miller, W. Allen
http://dx.doi.org/10.1146/annurev-micro-092412-155609
Source: Annu Rev Microbiol. 2013; 67:21-42.

[PDF-1.77 MB]

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Details:

Alternative Title:

Annu Rev Microbiol
Personal Author:

Simon, Anne E. ; Miller, W. Allen

Simon, Anne E. ; Miller, W. Allen Less -
Description:

In the absence of a 5' cap, plant positive-strand RNA viruses have evolved a number of different elements in their 3' untranslated region (UTR) to attract initiation factors and/or ribosomes to their templates. These 3' cap-independent translational enhancers (3' CITEs) take different forms, such as I-shaped, Y-shaped, T-shaped, or pseudoknotted structures, or radiate multiple helices from a central hub. Common features of most 3' CITEs include the ability to bind a component of the translation initiation factor eIF4F complex and to engage in an RNA-RNA kissing-loop interaction with a hairpin loop located at the 5' end of the RNA. The two T-shaped structures can bind to ribosomes and ribosomal subunits, with one structure also able to engage in a simultaneous long-distance RNA-RNA interaction. Several of these 3' CITEs are interchangeable and there is evidence that natural recombination allows exchange of modular CITE units, which may overcome genetic resistance or extend the virus's host range.
Subjects:

[+]

3' Untranslated Regions 3′ UTR Translation Elements Article EIF4E/eIF4G Internal Ribosome-binding Structures Long-distance RNA-RNA Interactions Noncanonical Translation Plant Viruses Protein Biosynthesis RNA, Viral RNA Caps RNA Structure And Function Viral Proteins
Source:

Annu Rev Microbiol. 2013; 67:21-42.
Pubmed ID:

23682606
Pubmed Central ID:

PMC4034384
Document Type:

Journal Article
Funding:

2 R01 GM067104/GM/NIGMS NIH HHS/United States ; GM 061515-05A2/G120CD/CD/ODCDC CDC HHS/United States ; GM 061515-07S1/GM/NIGMS NIH HHS/United States ; R01 GM067104/GM/NIGMS NIH HHS/United States

2 R01 GM067104/GM/NIGMS NIH HHS/United States ; GM 061515-05A2/G120CD/CD/ODCDC CDC HHS/United States ; GM 061515-07S1/GM/NIGMS NIH HHS/United States ; R01 GM067104/GM/NIGMS NIH HHS/United States Less -
Volume:

67
Collection(s):

CDC Public Access
Main Document Checksum:

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urn:sha256:1ec4ee0a1efe7ffa5622bb21685a929a0ecc6126eeb52bbfe6ca3f75c9e1cde8
Download URL:

https://stacks.cdc.gov/view/cdc/29969/cdc_29969_DS1.pdf
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