Open AccessSelective inhibition of RecA functions by the Hc1 nucleoid condensation protein from Chlamydia trachomatis
Author(s) -
Ennis Don G.,
Woodgate Roger,
Shi Mingxia
Publication year - 2000
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2000.tb08908.x
Subject(s) - nucleoid , chlamydia trachomatis , chromatin , biology , nucleoprotein , escherichia coli , recombination , microbiology and biotechnology , histone , mutant , dna , genetics , chemistry , virology , gene
During the normal biphasic life cycle of Chlamydia trachomatis , the histone‐like protein Hc1 promotes the condensation of nucleoids in elementary bodies, it may also displace nucleoproteins, including repair functions from chromatin. Hc1 was found to effectively inhibit the recombination and repair of the weak binding RecA430 mutant protein from Escherichia coli , but had minimal effects on the parental RecA + protein. Expression of Hc1 was also found to inhibit the repair activities of the C. trachomatis RecA protein but not recombination. These results suggest that chlamydial RecA may have evolved mechanisms to minimize Hc1 competition for recombinational activities.