Molecular basis distinguishing the DNA binding profile of nrf2-maf heterodimer from that of maf homodimer.

Molecular basis distinguishing the DNA binding profile of nrf2-maf heterodimer from that of maf homodimer. Research Abstract Details 

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Molecular basis distinguishing the DNA binding profile of nrf2-maf heterodimer from that of maf homodimer. Abstract Text:

Momoko Kimura,Tae Yamamoto,Jianyong Zhang,Ken Itoh,Motoki Kyo,Terue Kamiya,Hiroyuki Aburatani,Fumiki Katsuoka,Hirofumi Kurokawa,Toshiyuki Tanaka,Hozumi Motohashi,Masayuki Yamamoto,Momoko Kimura,Tae Yamamoto,Jianyong Zhang,Ken Itoh,Motoki Kyo,Terue Kamiya,Hiroyuki Aburatani,Fumiki Katsuoka,Hirofumi Kurokawa,Toshiyuki Tanaka,Hozumi Motohashi,Masayuki Yamamoto,Momoko Kimura,Tae Yamamoto,Jianyong Zhang,Ken Itoh,Motoki Kyo,Terue Kamiya,Hiroyuki Aburatani,Fumiki Katsuoka,Hirofumi Kurokawa,Toshiyuki Tanaka,Hozumi Motohashi,Masayuki Yamamoto,

Nrf2-small Maf heterodimer activates the transcription of many cytoprotective genes through the antioxidant response element and serves as a key factor in xenobiotic and oxidative stress responses. Our surface plasmon resonance-microarray binding analysis revealed that both Nrf2-MafG heterodimer and MafG homodimer bind to the consensus Maf recognition element with high affinity but bind differentially to the suboptimal binding sequences degenerated from the consensus. We examined the molecular basis distinguishing the binding profile of Nrf2-MafG heterodimer from that of MafG homodimer and found that the Ala-502 residue in the basic region of Nrf2 is a critical determinant of its binding specificity. In Maf proteins, a tyrosine resides in the position corresponding to Ala-502 in Nrf2. We prepared a mutant Nrf2 molecule in which Ala-502 was replaced with tyrosine. In surface plasmon resonance-microarray analysis, heterodimer of Nrf2(A502Y) and MafG displayed a binding specificity similar to that of MafG homodimer. The target genes activated by mutant Nrf2(A502Y)-small Maf heterodimer were largely different, albeit with some overlap, from those activated by wild-type Nrf2-small Maf, indicating that the array of target genes regulated by Nrf2-small Maf heterodimer differs substantially from that regulated by Maf homodimer in vivo. These results suggest that the distinct DNA binding profile of Nrf2-Maf heterodimer is biologically significant for Nrf2 to function as a key regulator of cytoprotective genes. Our contention is supported that the differential DNA binding specificity between Maf homodimers and Nrf2-Maf heterodimers establishes the differential gene regulation by these dimer-forming transcription factors.

Molecular basis distinguishing the DNA binding profile of nrf2-maf heterodimer from that of maf homodimer. Publishing Authors By Initials

M Kimura,T Yamamoto,J Zhang,K Itoh,M Kyo,T Kamiya,H Aburatani,F Katsuoka,H Kurokawa,T Tanaka,H Motohashi,M Yamamoto,M Kimura,T Yamamoto,J Zhang,K Itoh,M Kyo,T Kamiya,H Aburatani,F Katsuoka,H Kurokawa,T Tanaka,H Motohashi,M Yamamoto,M Kimura,T Yamamoto,J Zhang,K Itoh,M Kyo,T Kamiya,H Aburatani,F Katsuoka,H Kurokawa,T Tanaka,H Motohashi,M Yamamoto,

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Molecular basis distinguishing the DNA binding profile of nrf2-maf heterodimer from that of maf homodimer. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: The Journal of biological chemistry

VOLUME: 282

Page Numbers: 33681-90

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ISSN: 0021-9258

DAY: 17

MONTH: 09

YEAR: 2007

Molecular basis distinguishing the DNA binding profile of nrf2-maf heterodimer from that of maf homodimer. Information

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LANGUAGE: eng

NlmUniqueID: 2985121

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Grant and Affiliation Information for Molecular basis distinguishing the DNA binding profile of nrf2-maf heterodimer from that of maf homodimer.

AFFILIATION: Graduate School of Comprehensive Human Sciences and Center for Tsukuba Advanced Research Alliance and Graduate School of Life and Environmental Sciences, University of Tsukuba, 1-1-1 Tennoudai, Tsukuba 305-8572.

Country: United States

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MEDLINETA: J Biol Chem

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