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PMID: 2835510 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

The adenovirus tripartite leader may eliminate the requirement for cap-binding protein complex during translation initiation.

Journal of virology ·Vol. 62 ·No. 6 ·1988-06-00 ·Pages 2059-66

Dolph PJ, Racaniello V, Villamarin A, Palladino F, Schneider RJ

Abstract

The adenovirus tripartite leader is a 200-nucleotide 5' noncoding region that is found on all late viral mRNAs. This segment is required for preferential translation of viral mRNAs at late times during infection. Most tripartite leader-containing mRNAs appear to exhibit little if any requirement for intact cap-binding protein complex, a property previously established only for uncapped poliovirus mRNAs and capped mRNAs with minimal secondary structure. The tripartite leader also permits the translation of mRNAs in poliovirus-infected cells in the apparent absence of active cap-binding protein complex and does not require any adenovirus gene products for this activity. The preferential translation of viral late mRNAs may involve this unusual property.

MeSH Terms
Adenoviruses, Human/genetics Animals Carrier Proteins/physiology Cell Line Humans Macromolecular Substances Nucleic Acid Conformation Poliovirus/genetics Protein Biosynthesis RNA Cap-Binding Proteins RNA, Messenger/genetics RNA, Viral/genetics Time Factors Viral Proteins/genetics
Chemicals
Carrier Proteins Macromolecular Substances RNA Cap-Binding Proteins RNA, Messenger RNA, Viral Viral Proteins
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Dolph P J
Department of Biochemistry, New York University Medical Center, New York 10016.
Racaniello V
Villamarin A
Palladino F
Schneider R J
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Article Info
Journal
Journal of virology
Abbr.
J Virol
ISSN
0022-538X
Published
1988-06-00
Pages
2059-66
Language
English
Region
United States
NLM ID
0113724
PMCID
PMC253291
Subset
IM
Grants
NIAID NIH HHS · AI 20017 · United States
NCI NIH HHS · CA-42357 · United States
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