|PROSITE documentation PDOC00366|
The lacI-type HTH domain is a DNA-binding, helix-turn-helix (HTH) domain of about 50-60 residues present in the lacI/galR family of transcriptional regulators involved in metabolic regulation in prokaryotes. Most of these bacterial regulators recognize sugar-inducers. The family is named after the Escherichia coli lactose operon repressor lacI and galactose operon repressor galR. LacI-type regulators are present in diverse bacterial genera, in the cytoplasm. The 'helix-turn-helix' DNA-binding motif is located in the N-terminal extremity of these transcriptional regulators. The C-terminal part of lacI-type regulators contains several regions that can be involved in (1) binding of inducers, which are sugars and their analogs and (2) oligomerization. The lac repressor is a tetramer, whilst the gal and cyt repressors are dimers. LacI-type transcriptional regulators are important in the coordination of catabolic, metabolic and transport operons [1,2].
Several structures of lacI-type transcriptional regulators have been resolved and their DNA-binding domain encompasses a headpiece, formed by a fold of three helices, followed by a hinge region, which can form a fourth α helix or hinge-helix (see <PDB:1L1M>). The helix-turn-helix motif comprises the first and second helices, the second being called the recognition helix. The HTH is involved in DNA-binding into the major groove, while the hinge-helix fits into the minor groove and the complete domain specifically recognizes the operator DNA [3,4].
Some proteins known to contain a lacI-type HTH domain:
The pattern we developed spans the complete HTH motif, except for the last residue. We also developed a profile that covers the entire HTH and DNA-binding domain, including the hinge-helix and allows a more sensitive detection.Last update:
October 2003 / Text revised; profile added.
PROSITE methods (with tools and information) covered by this documentation:
|1||Authors||Vartak N.B. Reizer J. Reizer A. Gripp J.T. Groisman E.A. Wu L.-F. Tomich J.M. Saier M.H. Jr.|
|Title||Sequence and evolution of the FruR protein of Salmonella typhimurium: a pleiotropic transcriptional regulatory protein possessing both activator and repressor functions which is homologous to the periplasmic ribose-binding protein.|
|Source||Res. Microbiol. 142:951-963(1991).|
|2||Authors||Weickert M.J. Adhya S.|
|Title||A family of bacterial regulators homologous to Gal and Lac repressors.|
|Source||J. Biol. Chem. 267:15869-15874(1992).|
|3||Authors||Nguyen C.C. Saier M.H. Jr.|
|Title||Phylogenetic, structural and functional analyses of the LacI-GalR family of bacterial transcription factors.|
|Source||FEBS Lett. 377:98-102(1995).|
|Source||Curr. Opin. Microbiol. 1:145-151(1998).|