TY - JOUR
T1 - Less is more
T2 - Neisseria gonorrhoeae RecX protein stimulates recombination by inhibiting RecA
AU - Gruenig, Marielle C.
AU - Stohl, Elizabeth A.
AU - Chitteni-Pattu, Sindhu
AU - Seifert, H. Steven
AU - Cox, Michael M.
PY - 2010/11/26
Y1 - 2010/11/26
N2 - Escherichia coli RecX (RecXEc) is a negative regulator of RecA activities both in the bacterial cell and in vitro. In contrast, the Neisseria gonorrhoeae RecX protein (RecXNg) enhances all RecA-related processes in N. gonorrhoeae. Surprisingly, the RecXNg protein is not a RecA protein activator in vitro. Instead, RecXNg is a much more potent inhibitor of all RecANg and RecAEc activities than is the E. coli RecX ortholog. A series of RecXNg mutant proteins representing a gradient of functional deficiencies provide a direct correlation between RecANg inhibition in vitro and the enhancement of RecA Ng function in N. gonorrhoeae. Unlike RecXEc, RecX Ng does not simply cap the growing ends of RecA filaments, but it directly facilitates a more rapid RecA filament disassembly. Thus, in N. gonorrhoeae, recombinational processes are facilitated by RecXNg protein-mediated limitations on RecANg filament presence and/or length to achieve maximal function.
AB - Escherichia coli RecX (RecXEc) is a negative regulator of RecA activities both in the bacterial cell and in vitro. In contrast, the Neisseria gonorrhoeae RecX protein (RecXNg) enhances all RecA-related processes in N. gonorrhoeae. Surprisingly, the RecXNg protein is not a RecA protein activator in vitro. Instead, RecXNg is a much more potent inhibitor of all RecANg and RecAEc activities than is the E. coli RecX ortholog. A series of RecXNg mutant proteins representing a gradient of functional deficiencies provide a direct correlation between RecANg inhibition in vitro and the enhancement of RecA Ng function in N. gonorrhoeae. Unlike RecXEc, RecX Ng does not simply cap the growing ends of RecA filaments, but it directly facilitates a more rapid RecA filament disassembly. Thus, in N. gonorrhoeae, recombinational processes are facilitated by RecXNg protein-mediated limitations on RecANg filament presence and/or length to achieve maximal function.
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U2 - 10.1074/jbc.M110.171967
DO - 10.1074/jbc.M110.171967
M3 - Article
C2 - 20851893
AN - SCOPUS:78549267210
SN - 0021-9258
VL - 285
SP - 37188
EP - 37197
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 48
ER -