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PMID: 6313613 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Molecular cloning and expression of gene fragments from corynebacteriophage beta encoding enzymatically active peptides of diphtheria toxin.

Journal of bacteriology ·Vol. 156 ·No. 2 ·1983-11-00 ·Pages 680-5

Tweten RK, Collier RJ

Abstract

Two restriction fragments from corynebacteriophage beta vir tox+ that encode peptides similar to diphtheria toxin fragment A and the chain termination fragment, CRM45, have been cloned into Escherichia coli in plasmid pBR322. Clones containing the recombinant plasmids produced gene products that were active in catalyzing the ADP ribosylation of elongation factor 2 and were reactive with diphtheria toxin antiserum. Toxin-related peptides were found primarily in the periplasmic compartment and were degraded to nonimmunoreactive forms within 1 to 2 h of synthesis. The expression of both gene fragments appears to have originated from the diphtheria toxin promoter.

MeSH Terms
Bacteriophages/genetics Cloning, Molecular Corynebacterium diphtheriae/genetics DNA Restriction Enzymes Diphtheria Toxin/genetics,isolation & purification Genes Genes, Bacterial Genes, Viral Molecular Weight Nucleotidyltransferases/genetics,isolation & purification Poly(ADP-ribose) Polymerases
Chemicals
Diphtheria Toxin Poly(ADP-ribose) Polymerases Nucleotidyltransferases DNA Restriction Enzymes
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Tweten R K
Collier R J
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18 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
DOI
10.1128/jb.156.2.680-685.1983
Published
1983-11-00
Pages
680-5
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC217883
Subset
IM
Grants
NIAID NIH HHS · AI-07877 · United States
NIAID NIH HHS · AIO6855 · United States
External Links
PubMed source DOI: 10.1128/jb.156.2.680-685.1983 PMC Full Text View journal details
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