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.
journal_name
Proc Natl Acad Sci U S Aauthors
Isobe T,Black LW,Tsugita Adoi
10.1073/pnas.73.11.4205keywords:
subject
Has Abstractpub_date
1976-11-01 00:00:00pages
4205-9issue
11eissn
0027-8424issn
1091-6490journal_volume
73pub_type
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