Structure-activity analysis of microcinJ25: distinct parts of the threaded lasso molecule are responsible for interaction with bacterial RNA polymerase

Ekaterina Semenova; Yulia Yuzenkova; Jean Peduzzi; Sylvie Rebuffat; Konstantin Severinov

doi:10.1128/JB.187.11.3859-3863.2005

Structure-activity analysis of microcinJ25: distinct parts of the threaded lasso molecule are responsible for interaction with bacterial RNA polymerase

J Bacteriol. 2005 Jun;187(11):3859-63. doi: 10.1128/JB.187.11.3859-3863.2005.

Authors

Ekaterina Semenova¹, Yulia Yuzenkova, Jean Peduzzi, Sylvie Rebuffat, Konstantin Severinov

Affiliation

¹ Waksman Institute for Microbiology, Department of Molecular Biology and Biochemistry, Rutgers, The State University of New Jersey, 190 Frelinghuysen Road, Piscataway, New Jersey 08854, USA.

Abstract

Peptide microcin J25 (MccJ25) inhibits bacterial RNA polymerase. We show that thermolysin-cleaved MccJ25 and MccJ25 lacking amino acids 13 to 17 also inhibit transcription. Our data and structural analysis of intact and thermolysin-digested MccJ25 suggest that distinct regions of MccJ25 are involved in transcription inhibition and cell entry.

Publication types

Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

MeSH terms

Amino Acid Sequence
Bacteriocins / chemistry*
Bacteriocins / metabolism*
DNA-Directed RNA Polymerases / metabolism*
Escherichia coli / enzymology*
Escherichia coli / genetics
Escherichia coli Proteins / genetics
Escherichia coli Proteins / metabolism*
Molecular Sequence Data
Protein Structure, Tertiary
Structure-Activity Relationship
Thermolysin
Transcription, Genetic

Substances

Bacteriocins
Escherichia coli Proteins
microcin
DNA-Directed RNA Polymerases
Thermolysin

Abstract

Publication types

MeSH terms

Substances

Grants and funding