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PMID: 1069310 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Protein cleavage during virus assembly: a novel specificity of assembly dependent cleavage in bacteriophage T4.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 73 ·No. 11 ·1976-11-00 ·Pages 4205-9

Isobe T, Black LW, Tsugita A

Abstract

Cleavage of precursor proteins occurs during assembly of numerous viruses. Seven bacteriophage T4 head-related proteins areknown to be cleaved during morphogenesis. Sequences surrounding the cleavage sites in T4 head precursors P23 and IPIII are reported here. We previously determined the sequences of precursor and processed forms of IPII and IPI. Cleavage occurs at a glutamyl-alanyl bond in each protein. By comparison of sequences around five cleaved and four uncleaved Glu-Ala bonds in head precursors, it appears that cleavage is limited to the Thr or Ala, and X2 to hydrophilic residues. The results suggest the viral-induced assembly protease recognizes and cleaves an extended primary structure in the structurally dissimilar precursors.

MeSH Terms
Amino Acid Sequence Coliphages/enzymology,metabolism Endopeptidases/metabolism Protein Precursors/metabolism Viral Proteins/metabolism Virus Replication
Chemicals
Protein Precursors Viral Proteins Endopeptidases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Isobe T
Black L W
Tsugita A
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25 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.73.11.4205
Published
1976-11-00
Pages
4205-9
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC431386
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.73.11.4205 PMC Full Text View journal details
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