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PMID: 3469652 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Cloning and purification of a unique lysozyme produced by Bacillus phage phi 29.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 84 ·No. 4 ·1987-02-00 ·Pages 955-8

Saedi MS, Garvey KJ, Ito J

Abstract

A DNA fragment of the bacteriophage phi 29 chromosome, encoding the entire sequence of phi 29 gene 15, has been cloned into the Escherichia coli expression vector pPLc245 under the control of the phage lambda major leftward promoter, PL. Upon heat induction, a protein with an apparent molecular mass of 26 kDa was overproduced. The molecular mass of this protein corresponds to the 28 kDa predicted for the product of gene 15 from its nucleotide sequence. The overproduced protein has been purified to near homogeneity and confirmed to be the product of gene 15 by amino acid sequence analysis of its N terminus. The purified product of gene 15 has a lysozyme activity similar to other phage-type lysozymes: products of phage T4 gene e and of phage P22 gene 19. However, to our knowledge phi 29 lysozyme is structurally unique among the phage-type lysozymes.

MeSH Terms
Amino Acid Sequence Bacillus/enzymology Bacteriophages Cloning, Molecular Genes Muramidase/genetics,isolation & purification
Chemicals
Muramidase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Saedi M S
Garvey K J
Ito J
References (18)
18 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.84.4.955
Published
1987-02-00
Pages
955-8
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC304338
Subset
IM
Grants
NIGMS NIH HHS · GM28013 · United States
External Links
PubMed source DOI: 10.1073/pnas.84.4.955 PMC Full Text View journal details
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