The endolysin-binding domain encompasses the N-terminal region of the mycobacteriophage Ms6 Gp1 chaperone

J Bacteriol. 2011 Sep;193(18):5002-6. doi: 10.1128/JB.00380-11. Epub 2011 Jul 15.

Abstract

The intermolecular interactions of the mycobacteriophage Ms6 secretion chaperone with endolysin were characterized. The 384-amino-acid lysin (lysin(384))-binding domain was found to encompass the N-terminal region of Gp1, which is also essential for a lysis phenotype in Escherichia coli. In addition, a GXXXG-like motif involved in Gp1 homo-oligomerization was identified within the C-terminal region.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Bacteriolysis
  • Endopeptidases / genetics
  • Endopeptidases / metabolism*
  • Escherichia coli / physiology
  • Molecular Chaperones / genetics
  • Molecular Chaperones / metabolism*
  • Molecular Sequence Data
  • Mycobacteriophages / genetics
  • Mycobacteriophages / metabolism*
  • Protein Binding
  • Protein Interaction Mapping*
  • Protein Multimerization
  • Sequence Alignment
  • Viral Proteins / genetics
  • Viral Proteins / metabolism*

Substances

  • Molecular Chaperones
  • Viral Proteins
  • Endopeptidases
  • endolysin