The Escherichia coli hflA locus encodes a putative GTP-binding protein and two membrane proteins, one of which contains a protease-like domain.

AUTOR(ES)

Noble, J A

RESUMO

The hflA (high frequency of lysogenization) locus of Escherichia coli governs the lysis-lysogeny decision of bacteriophage lambda by controlling stability of the phage cII protein. hflA contains three genes, hflX, hflK, and hflC, encoding polypeptides of 50, 46, and 37 kDa, respectively. We have determined the nucleotide sequence of 3843 base pairs containing hflA and have found three large open reading frames corresponding to hflX, hflK, and hflC. HflX contains the three sequence motifs typical of GTP-binding proteins and appears to be a member of a distinct family of putative GTPases. HflC and HflK appear to be integral membrane proteins which show some similarity to each other and to a human membrane protein. The C-terminal region of HflC contains a domain resembling the catalytic domain of ClpP, a bacterial ATP-dependent protease. We hypothesize that HflK and HflC constitute a distinct membrane-bound protease whose activity may be modulated by HflX GTPase.

Documentos Relacionados

• Membrane localization of the HflA regulatory protease of Escherichia coli by immunoelectron microscopy.
• Relocation of a protease-like gene segment between two retroviruses.
• Small GTP-Binding Proteins and Membrane Biogenesis in Plants.
• A GTP-binding protein of Escherichia coli has homology to yeast RAS proteins.
• Characterization of membrane-bound small GTP-binding proteins from Nicotiana tabacum.