Skip to main content

Some NLM-NCBI services and products are experiencing heavy traffic, which may affect performance and availability. We apologize for the inconvenience and appreciate your patience. For assistance, please contact our Help Desk at info@ncbi.nlm.nih.gov.

Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1976 Nov;73(11):4205–4209. doi: 10.1073/pnas.73.11.4205

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

T Isobe, L W Black, A Tsugita
PMCID: PMC431386  PMID: 1069310

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.

Full text

PDF
4205

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Black L. W. Ahmad-Zadeh C,+AHMADAAZADEH C: Internal proteins of bacteriophage T4D: their characterization and relation to head structure and assembly. J Mol Biol. 1971 Apr 14;57(1):71–92. doi: 10.1016/0022-2836(71)90120-3. [DOI] [PubMed] [Google Scholar]
  2. Black L. W. Bacteriophage T4 internal protein mutants: isolation and properties. Virology. 1974 Jul;60(1):166–179. doi: 10.1016/0042-6822(74)90374-2. [DOI] [PubMed] [Google Scholar]
  3. Braunitzer G., Schrank B., Ruhfus A. Zum vollständigen und autoatischen Abbau von Peptiden nach der Quadrolmethode. Hoppe Seylers Z Physiol Chem. 1970 Dec;351(12):1589–1590. [PubMed] [Google Scholar]
  4. Casjens S., King J. Virus assembly. Annu Rev Biochem. 1975;44:555–611. doi: 10.1146/annurev.bi.44.070175.003011. [DOI] [PubMed] [Google Scholar]
  5. Celis J. E., Smith J. D., Brenner S. Correlation between genetic and translational maps of gene 23 in bacteriophage T4. Nat New Biol. 1973 Jan 31;241(109):130–132. doi: 10.1038/newbio241130a0. [DOI] [PubMed] [Google Scholar]
  6. Chou P. Y., Fasman G. D. Prediction of protein conformation. Biochemistry. 1974 Jan 15;13(2):222–245. doi: 10.1021/bi00699a002. [DOI] [PubMed] [Google Scholar]
  7. Dickson R. C., Barnes S. L., Eiserling F. A. Structural proteins of bacteriophage T4. J Mol Biol. 1970 Nov 14;53(3):461–474. doi: 10.1016/0022-2836(70)90077-x. [DOI] [PubMed] [Google Scholar]
  8. Giri J. G., McCullough J. E., Champe S. P. Identification of gene products required for in vitro formation of the internal peptides of bacteriophage T4. J Virol. 1976 Jun;18(3):894–903. doi: 10.1128/jvi.18.3.894-903.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Goldstein J., Champe S. P. T4-induced activity required for specific cleavage of a bacteriophage protein in vitro. J Virol. 1974 Feb;13(2):419–427. doi: 10.1128/jvi.13.2.419-427.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Hershko A., Fry M. Post-translational cleavage of polypeptide chains: role in assembly. Annu Rev Biochem. 1975;44:775–797. doi: 10.1146/annurev.bi.44.070175.004015. [DOI] [PubMed] [Google Scholar]
  11. Horvitz H. R. Bacteriophage T4 mutants deficient in alteration and modification of the Escherichia coli RNA polymerase. J Mol Biol. 1974 Dec 25;90(4):739–750. doi: 10.1016/0022-2836(74)90537-3. [DOI] [PubMed] [Google Scholar]
  12. Hosoda J., Cone R. Analysis of T4 phage proteins. I. Conversion of precursor proteins into lower molecular weight peptides during normal capsid formation. Proc Natl Acad Sci U S A. 1970 Aug;66(4):1275–1281. doi: 10.1073/pnas.66.4.1275. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Isobe T., Black L. W., Tsugita A. Primary structure of bacteriophage T4 internal protein II and characterization of the cleavage upon phage maturation. J Mol Biol. 1976 Apr 5;102(2):349–365. doi: 10.1016/s0022-2836(76)80059-9. [DOI] [PubMed] [Google Scholar]
  14. Kellenberger E., Der Kamp C. K.-V. On a modification of the gene product P23 according to its use as subunit of either normal capsids of phage T4 or of polyheads. FEBS Lett. 1970 Jun 1;8(3):140–144. doi: 10.1016/0014-5793(70)80247-2. [DOI] [PubMed] [Google Scholar]
  15. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  16. Lim V. I. Algorithms for prediction of alpha-helical and beta-structural regions in globular proteins. J Mol Biol. 1974 Oct 5;88(4):873–894. doi: 10.1016/0022-2836(74)90405-7. [DOI] [PubMed] [Google Scholar]
  17. Lim V. I. Structural principles of the globular organization of protein chains. A stereochemical theory of globular protein secondary structure. J Mol Biol. 1974 Oct 5;88(4):857–872. doi: 10.1016/0022-2836(74)90404-5. [DOI] [PubMed] [Google Scholar]
  18. Matthews B. W., Remington S. J. The three dimensional structure of the lysozyme from bacteriophage T4. Proc Natl Acad Sci U S A. 1974 Oct;71(10):4178–4182. doi: 10.1073/pnas.71.10.4178. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Mendez E., Lai C. Y. Regeneration of amino acids from thiazolinones formed in the Edman degradation. Anal Biochem. 1975 Sep;68(1):47–53. doi: 10.1016/0003-2697(75)90677-6. [DOI] [PubMed] [Google Scholar]
  20. Onorato L., Showe M. K. Gene 21 protein-dependent proteolysis in vitro of purified gene 22 product of bacteriophage T4. J Mol Biol. 1975 Mar 5;92(3):395–412. doi: 10.1016/0022-2836(75)90288-0. [DOI] [PubMed] [Google Scholar]
  21. SARABHAI A. S., STRETTON A. O., BRENNER S., BOLLE A. CO-LINEARITY OF THE GENE WITH THE POLYPEPTIDE CHAIN. Nature. 1964 Jan 4;201:13–17. doi: 10.1038/201013a0. [DOI] [PubMed] [Google Scholar]
  22. Showe M. K., Black L. W. Assembly core of bacteriophage T4: an intermediate in head formation. Nat New Biol. 1973 Mar 21;242(116):70–75. doi: 10.1038/newbio242070a0. [DOI] [PubMed] [Google Scholar]
  23. Summers M. R., Smythers G. W., Oroszlan S. Thin-layer chromatography of sub-nanomole amounts of phenylthiohydantoin (PTH) amino acids on polyamide sheets. Anal Biochem. 1973 Jun;53(2):624–628. doi: 10.1016/0003-2697(73)90114-0. [DOI] [PubMed] [Google Scholar]
  24. Tsugita A., Inouye M. Complete primary structure of phage lysozyme from Escherichia coli T4. J Mol Biol. 1968 Oct 14;37(1):201–212. doi: 10.1016/0022-2836(68)90083-1. [DOI] [PubMed] [Google Scholar]
  25. van Eerd J. P., Takahshi K. Determination of the complete amino acid sequence of bovine cardiac troponin C. Biochemistry. 1976 Mar 9;15(5):1171–1180. doi: 10.1021/bi00650a033. [DOI] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES