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Solution structure of the 13th C2H2 Zinc Finger of Miz-1.

Tremblay C, Bédard M, Bonin MA, Lavigne P
Biochem Biophys Res Commun 473 471-5 (2016)
Related entries: 2n25, 2n26

Cited: 3 times
EuropePMC logo PMID: 26972249

Abstract

Miz-1 is a BTB/POZ transcription factor that contains 13C2H2 Zinc Finger domains (ZF). Miz-1 transactivates and represses the transcription of a myriad of genes involved in many aspects of the biology of the cell. The detailed molecular interactions through which Miz-1 controls transcription, including its specific DNA binding via its ZF domains, remain to be understood and documented. In our effort to shed light into the structural biology of Miz-1, we have undertaken the determination of the structure of all its ZF and the characterization of their interactions with cognate DNA. The structure of ZF 1 to 10 have already been solved and characterized. Here, we present the structure of the synthetic Miz-1 ZF13 determined by 2D (1)H-(1)H NMR.

Articles citing this publication (3)

  1. Exploring potential roles for the interaction of MOM1 with SUMO and the SUMO E3 ligase-like protein PIAL2 in transcriptional silencing. Zhao QY, He XJ. PLoS One 13 e0202137 (2018)
  2. Staphylococcus aureus Prophage-Encoded Protein Causes Abortive Infection and Provides Population Immunity against Kayviruses. Kuntová L, Mašlaňová I, Obořilová R, Šimečková H, Finstrlová A, Bárdy P, Šiborová M, Troianovska L, Botka T, Gintar P, Šedo O, Farka Z, Doškař J, Pantůček R. mBio 14 e0249022 (2023)
  3. NMR structure verifies the eponymous zinc finger domain of transcription factor ZNF750. Rua AJ, Whitehead RD, Alexandrescu AT. J Struct Biol X 8 100093 (2023)


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