Characterization of the Streptococcus suis XerS recombinase and its unconventional cleavage of the difSL site.
FEMS Microbiol Lett
; 324(2): 135-41, 2011 Nov.
Article
en En
| MEDLINE
| ID: mdl-22092814
ABSTRACT
XerC and XerD are members of the tyrosine recombinase family and mediate site-specific recombination that contributes to the stability of circular chromosomes in bacteria by resolving plasmid multimers and chromosome dimers to monomers prior to cell division. Homologues of xerC/xerD genes have been found in many bacteria, and in the lactococci and streptococci, a single recombinase called XerS can perform the functions of XerC and XerD. The xerS gene of Streptococcus suis was cloned, overexpressed and purified as a maltose-binding protein (MBP) fusion. The purified MBP-XerS fusion showed specific DNA-binding activity to both halves of the dif site of S. suis, and covalent protein-DNA complexes were also detected with dif site suicide substrates. These substrates were also cleaved in a specific fashion by MBP-XerS, generating cleavage products separated by an 11-bp spacer region, unlike the traditional 6-8-bp spacer observed in most tyrosine recombinases. Furthermore, xerS mutants of S. suis showed significant growth and morphological changes.
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1
Banco de datos:
MEDLINE
Asunto principal:
Proteínas Bacterianas
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ADN Bacteriano
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Streptococcus suis
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Recombinasas
Idioma:
En
Año:
2011
Tipo del documento:
Article