Properties of HflX, an Enigmatic Protein from Escherichia coli

被引：24

作者：

Dutta, Dipak ^{[1
]}

Bandyopadhyay, Kaustav ^{[1
]}

Datta, Ajit Bikram ^{[1
]}

Sardesai, Abhijit A. ^{[2
]}

Parrack, Pradeep ^{[1
]}

机构：

[1] Bose Inst, Dept Biochem, Kolkata 700054, India

[2] Ctr DNA Fingerprinting & Diag, Hyderabad 500076, Andhra Pradesh, India

来源：

JOURNAL OF BACTERIOLOGY | 2009年 / 191卷 / 07期

关键词：

SECONDARY STRUCTURE PREDICTION; CIRCULAR-DICHROISM SPECTRA; TRANSFER-RNA MODIFICATION; LYSIS-LYSOGENY DECISION; GTP-BINDING PROTEIN; BACTERIOPHAGE-LAMBDA; FTSH HFLB; PHAGE-LAMBDA; MISMATCH REPAIR; HEAT-SHOCK;

D O I：

10.1128/JB.01353-08

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

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.

引用

页码：2307 / 2314

页数：8

共 56 条

[1] EVALUATION OF SECONDARY STRUCTURE OF PROTEINS FROM UV CIRCULAR-DICHROISM SPECTRA USING AN UNSUPERVISED LEARNING NEURAL-NETWORK [J].