Maf recognition element gene transcriptions: Difference between revisions

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Large "and small [musculoaponeurotic fibrosarcoma] Maf proteins are able to form homodimers that recognize the Maf recognition element (MARE)."<ref name=Otsuki>{{ cite journal
Large "and small [musculoaponeurotic fibrosarcoma] Maf proteins are able to form homodimers that recognize the Maf recognition element (MARE)."<ref name=Otsuki>{{ cite journal
|authors=Akihito Otsuki, Mikiko Suzuki, Fumiki Katsuoka, Kouhei Tsuchida, Hiromi Suda, Masanobu Morita, Ritsuko Shimizu, Masayuki Yamamoto
|author=Akihito Otsuki, Mikiko Suzuki, Fumiki Katsuoka, Kouhei Tsuchida, Hiromi Suda, Masanobu Morita, Ritsuko Shimizu, Masayuki Yamamoto
|title=Unique cistrome defined as CsMBE is strictly required for Nrf2-sMaf heterodimer function in cytoprotection
|title=Unique cistrome defined as CsMBE is strictly required for Nrf2-sMaf heterodimer function in cytoprotection
|journal=Free Radical Biology and Medicine
|journal=Free Radical Biology and Medicine
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|accessdate=21 August 2020 }}</ref>
|accessdate=21 August 2020 }}</ref>


bZIP Maf is a domain found in Maf [[transcription factor]] [[protein]]s that contains a [[leucine zipper]] (bZIP) domain, which mediates the transcription factor's dimerization and DNA binding properties with DNA motifs termed the Maf recognition elements (MAREs) that are 13 or 14 [[base pairs]] long such that the two residues at the beginning of [[helix]] H2 are positioned to recognize the flanking region of the DNA.<ref name=Kusunoki>{{ cite journal |authors=Kusunoki H, Motohashi H, Katsuoka F, Morohashi A, Yamamoto M, Tanaka T
bZIP Maf is a domain found in Maf [[transcription factor]] [[protein]]s that contains a [[leucine zipper]] (bZIP) domain, which mediates the transcription factor's dimerization and DNA binding properties with DNA motifs termed the Maf recognition elements (MAREs) that are 13 or 14 [[base pairs]] long such that the two residues at the beginning of [[helix]] H2 are positioned to recognize the flanking region of the DNA.<ref name=Kusunoki>{{ cite journal |author=Kusunoki H, Motohashi H, Katsuoka F, Morohashi A, Yamamoto M, Tanaka T
| title = Solution structure of the DNA-binding domain of MafG
| title = Solution structure of the DNA-binding domain of MafG
| journal = Nat. Struct. Biol.
| journal = Nat. Struct. Biol.
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"Maf factors recognize relatively long palindromic DNA sequences, TGCTGA(G/C)TCAGCA and TGCTGA(GC/CG)TCAGCA, which are now known as Maf recognition elements (MAREs)."<ref name=Kyo>{{ cite journal
"Maf factors recognize relatively long palindromic DNA sequences, TGCTGA(G/C)TCAGCA and TGCTGA(GC/CG)TCAGCA, which are now known as Maf recognition elements (MAREs)."<ref name=Kyo>{{ cite journal
|authors=Motoki Kyo, Tae Yamamoto, Hozumi Motohashi, Terue Kamiya, Toshihiro Kuroita, Toshiyuki Tanaka, James Douglas Engel, Bunsei Kawakami, Masayuki Yamamoto
|author=Motoki Kyo, Tae Yamamoto, Hozumi Motohashi, Terue Kamiya, Toshihiro Kuroita, Toshiyuki Tanaka, James Douglas Engel, Bunsei Kawakami, Masayuki Yamamoto
|title=Evaluation of MafG interaction with Maf recognition element arrays by surface plasmon resonance imaging technique
|title=Evaluation of MafG interaction with Maf recognition element arrays by surface plasmon resonance imaging technique
|journal=Genes to Cells
|journal=Genes to Cells

Revision as of 22:21, 13 September 2020

Associate Editor(s)-in-Chief: Henry A. Hoff

Large "and small [musculoaponeurotic fibrosarcoma] Maf proteins are able to form homodimers that recognize the Maf recognition element (MARE)."[1]

bZIP Maf is a domain found in Maf transcription factor proteins that contains a leucine zipper (bZIP) domain, which mediates the transcription factor's dimerization and DNA binding properties with DNA motifs termed the Maf recognition elements (MAREs) that are 13 or 14 base pairs long such that the two residues at the beginning of helix H2 are positioned to recognize the flanking region of the DNA.[2]

Human genes

Interactions

Consensus sequences

"Maf factors recognize relatively long palindromic DNA sequences, TGCTGA(G/C)TCAGCA and TGCTGA(GC/CG)TCAGCA, which are now known as Maf recognition elements (MAREs)."[3]

Samplings

Copying an apparent consensus sequence for the MARE of TGCTGA or TCAGCA and putting it in "⌘F" finds none located between ZSCAN22 and A1BG but using TCAGCA alone finds five between ZNF497 and A1BG as can be found by the computer programs.

See also

References

  1. Akihito Otsuki, Mikiko Suzuki, Fumiki Katsuoka, Kouhei Tsuchida, Hiromi Suda, Masanobu Morita, Ritsuko Shimizu, Masayuki Yamamoto (February 2016). "Unique cistrome defined as CsMBE is strictly required for Nrf2-sMaf heterodimer function in cytoprotection". Free Radical Biology and Medicine. 91: 45–57. doi:10.1016/j.freeradbiomed.2015.12.005. PMID 26677805. Retrieved 21 August 2020.
  2. Kusunoki H, Motohashi H, Katsuoka F, Morohashi A, Yamamoto M, Tanaka T (April 2002). "Solution structure of the DNA-binding domain of MafG". Nat. Struct. Biol. 9 (4): 252–6. doi:10.1038/nsb771. PMID 11875518.
  3. Motoki Kyo, Tae Yamamoto, Hozumi Motohashi, Terue Kamiya, Toshihiro Kuroita, Toshiyuki Tanaka, James Douglas Engel, Bunsei Kawakami, Masayuki Yamamoto (13 February 2004). "Evaluation of MafG interaction with Maf recognition element arrays by surface plasmon resonance imaging technique". Genes to Cells. 9 (2). doi:10.1111/j.1356-9597.2004.00711.x. Retrieved 8 September 2020.

External links