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

Maria João Catalão; Filipa Gil; José Moniz-Pereira; Madalena Pimentel

doi:10.1128/JB.00380-11

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.

Authors

Maria João Catalão¹, Filipa Gil, José Moniz-Pereira, Madalena Pimentel

Affiliation

¹ Centro de Patogénese Molecular, Unidade dos Retrovírus e Infecções Associadas, Faculty of Pharmacy, University of Lisbon, Av. Prof. Gama Pinto, 1649-003 Lisbon, Portugal.

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