Properties of HflX, an enigmatic protein from Escherichia coli.
The Escherichia coli gene hflX was first identified as part of the hflA operon, mutations in which led to an increased frequency of lysogenization upon infection of the bacterium by the temperate coliphage lambda. Independent mutational studies have also indicated that the HflX protein has a role in transposition. Based on the sequence of its gene, HflX is predicted to be a GTP-binding protein, very likely a GTPase. We report here purification and characterization of the HflX protein. We also specifically examined its suggested functional roles mentioned above. Our results show that HflX is a monomeric protein with a high (30% to 40%) content of helices. It exhibits GTPase as well as ATPase activities, but it has no role in lambda lysogeny or in transposition.
Dutta
Dipak
D
Department of Biochemistry, Bose Institute, Kolkata, India.
Bandyopadhyay
Kaustav
K
Datta
Ajit Bikram
AB
Sardesai
Abhijit A
AA
Parrack
Pradeep
P
D000251:Adenosine Triphosphatases / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D010582:Bacteriophage lambda / Q000502:physiology; D004926:Escherichia coli / Q000737:chemistry / Q000235:genetics / Q000378:metabolism* / Q000821:virology; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D020558:GTP Phosphohydrolases / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D019204:GTP-Binding Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D008242:Lysogeny
D029968:Escherichia coli Proteins; D000251:Adenosine Triphosphatases; D020558:GTP Phosphohydrolases; D019204:GTP-Binding Proteins; C535071:HflX protein, E coli