Literature DB >> 6295443

Phage P22 tail protein: gene and amino acid sequence.

R T Sauer, W Krovatin, A R Poteete, P B Berget.   

Abstract

The tail structure of the Salmonella phage P22 mediates both adsorption of the phage to its host and enzymatic hydrolysis of the bacterial O-antigen. The tail is an oligomeric structure, which is assembled from a single polypeptide species. We report here the amino- and carboxyl-terminal sequences of the P22 tail protein and the nucleotide sequence of its gene (gene 9). These data specify the complete amino acid sequence of the tail protein. The tail protein is a slightly acidic protein containing 666 amino acids. Comparison of the gene and protein sequences indicates that mature tail protein arises by cleavage of the initiator N-formyl-methionine from the nascent chain.

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Year:  1982        PMID: 6295443     DOI: 10.1021/bi00266a014

Source DB:  PubMed          Journal:  Biochemistry        ISSN: 0006-2960            Impact factor:   3.162


  22 in total

1.  Beta-helix core packing within the triple-stranded oligomerization domain of the P22 tailspike.

Authors:  J F Kreisberg; S D Betts; J King
Journal:  Protein Sci       Date:  2000-12       Impact factor: 6.725

2.  Pressure dissociation studies provide insight into oligomerization competence of temperature-sensitive folding mutants of P22 tailspike.

Authors:  Brian G Lefebvre; Noelle K Comolli; Matthew J Gage; Anne Skaja Robinson
Journal:  Protein Sci       Date:  2004-05-07       Impact factor: 6.725

3.  Intragenic suppressors of folding defects in the P22 tailspike protein.

Authors:  B Fane; J King
Journal:  Genetics       Date:  1991-02       Impact factor: 4.562

4.  Cold rescue of the thermolabile tailspike intermediate at the junction between productive folding and off-pathway aggregation.

Authors:  S D Betts; J King
Journal:  Protein Sci       Date:  1998-07       Impact factor: 6.725

5.  Identification of sites influencing the folding and subunit assembly of the P22 tailspike polypeptide chain using nonsense mutations.

Authors:  B Fane; J King
Journal:  Genetics       Date:  1987-10       Impact factor: 4.562

6.  Modulation of Escherichia coli RecBCD activity by the bacteriophage lambda Gam and P22 Abc functions.

Authors:  A R Poteete; A C Fenton; K C Murphy
Journal:  J Bacteriol       Date:  1988-05       Impact factor: 3.490

7.  The interdigitated beta-helix domain of the P22 tailspike protein acts as a molecular clamp in trimer stabilization.

Authors:  Jason F Kreisberg; Scott D Betts; Cameron Haase-Pettingell; Jonathan King
Journal:  Protein Sci       Date:  2002-04       Impact factor: 6.725

8.  Bacteriophage P22 gene 23 product acts preferentially in cis.

Authors:  P D Riggs; D Botstein
Journal:  J Virol       Date:  1987-07       Impact factor: 5.103

9.  The effects of mutations in the ant promoter of phage P22 depend on context.

Authors:  D Graña; T Gardella; M M Susskind
Journal:  Genetics       Date:  1988-10       Impact factor: 4.562

10.  Phage P22 tailspike protein: removal of head-binding domain unmasks effects of folding mutations on native-state thermal stability.

Authors:  S Miller; B Schuler; R Seckler
Journal:  Protein Sci       Date:  1998-10       Impact factor: 6.725

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