|PROSITE documentation PDOC00477 [for PROSITE entry PS50937]|
The merR-type HTH domain is a DNA-binding, winged helix-turn-helix (wHTH) domain of about 70 residues present in the merR family of transcriptional regulators. The family is named after the merR regulator of mercury resistance operons of Gram-negative bacteria found on transposons Tn21 and Tn501 . MerR-type regulators are present in diverse bacterial genera, in the cytoplasm. The helix-turn-helix DNA-binding motif is located in the N-terminal part of these transcriptional regulators and is followed by a coiled-coil region. The C-terminal part of merR-type regulators contains effector binding regions that are specific to the effector recognized. Most merR-type transcriptional regulators respond to environmental stimuli, like heavy metals, oxidative stress or antibiotics and a subgroup of metalloregulators are bacterial transcription activators that respond to metal ions .
Several structures of merR-type transcriptional regulators have been resolved and their N-terminal DNA-binding domains are ascribed to the superfamily of winged-helix proteins, containing a four-helix (H) bundle and a three-stranded antiparallel β-sheet (B) in the topology: B1-H1-H2-B2-B3-H3-H4 (see <PDB:1JBG>) . 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, where the recognition helix makes most DNA-contacts. The second DNA-binding element is wing W1, composed of the second and third β-strands and their connecting loop. The third DNA-binding element, wing W2, is not a loop like in typical winged-helix proteins, but another H-T-H motif formed by helices three and four. In a typical merR regulator, the HTH and two wings bind the promoter of the regulated operon between the -35 and -10 regions in a spacer of 19/20 bp and longer than usual, distorting the operator DNA and causing RNA polymerase to initiate transcription . Most merR-like transcriptional regulators are dimers.
Some proteins known to contain a merR-type HTH domain:
The pattern we developed starts at position 2 of the helix-turn-helix motif and extends three residues upstream of its C-terminal extremity. We also developed a profile that covers the entire wHTH, including the first strand, H-T-H motif, wings W1 and W2 and which 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||Helmann J.D. Wang Y. Mahler I. Walsh C.T.|
|Title||Homologous metalloregulatory proteins from both gram-positive and gram-negative bacteria control transcription of mercury resistance operons.|
|Source||J. Bacteriol. 171:222-229(1989).|
|2||Authors||Brown N.L. Stoyanov J.V. Kidd S.P. Hobman J.L.|
|Title||The MerR family of transcriptional regulators.|
|Source||FEMS Microbiol. Rev. 27:145-163(2003).|
|3||Authors||Zheleznova-Heldwein E.E. Brennan R.G.|