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- W997601162 abstract "Two putative oxidative-stress sensor proteins from Pseudomonas aeruginosa, PA1607 and PA1374, belong to the MarR family of transcription regulators and possess a unique mode of dimerization. In these proteins, in addition to the α-helices involved in dimerization, inter-subunit contacts are strengthened by additional C-terminal β-strands. Using sequence and structure analysis we show that these β-strands constitute a novel segment-swapped zinc ribbon domain. We detect the presence of the zinc ribbon domain in MarR proteins from many bacterial homologs. While the metal-chelating residues of the zinc ribbons are absent in most members of this family, we could however identify several species of Proteobacteria, Actinobacteria and Firmicutes that possess intact zinc-chelating sites. Conservation pattern of metal-chelating residues together with the extensive structural resemblance to zinc ribbons, in particular to the bridge-region of the dsDNA break repair protein Ku, suggests that the C-terminal β-rich region of these proteins is a zinc ribbon. Sequence analysis also supports a distant evolutionary connection between the zinc ribbons of the MarR and Ku families. However, unlike Ku where the segment-swapped zinc ribbons play a role in DNA-binding and obligate dimerization, their primary role in MarR appears to be in dimerization and strengthening of inter-subunit contacts." @default.
- W997601162 created "2016-06-24" @default.
- W997601162 creator A5017697005 @default.
- W997601162 creator A5074085320 @default.
- W997601162 date "2015-09-01" @default.
- W997601162 modified "2023-09-26" @default.
- W997601162 title "The Ku–Mar zinc finger: A segment-swapped zinc ribbon in MarR-like transcription regulators related to the Ku bridge" @default.
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- W997601162 doi "https://doi.org/10.1016/j.jsb.2015.07.011" @default.
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