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

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.

authors

Isobe T,Black LW,Tsugita A

doi

10.1073/pnas.73.11.4205

keywords:

subject

Has Abstract

pub_date

1976-11-01 00:00:00

pages

4205-9

issue

11

eissn

0027-8424

issn

1091-6490

journal_volume

73

pub_type

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