PF01753

MYND finger

Pfam entry
Member databasePfam
Pfam typedomain
Short namezf-MYND
ClanTRASH
Author Bateman A;0000-0002-6982-4660
Sequence Ontology0000417

Description
Imported from IPR002893

Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead binding other metals such as iron, or no metal at all. For example, some family members form salt bridges to stabilise the finger-like folds. They were first identified as a DNA-binding motif in transcription factor TFIIIA from Xenopus laevis (African clawed frog), however they are now recognised to bind DNA, RNA, protein and/or lipid substrates
[1, 2, 3, 8, 13]
. Their binding properties depend on the amino acid sequence of the finger domains and of the linker between fingers, as well as on the higher-order structures and the number of fingers. Znf domains are often found in clusters, where fingers can have different binding specificities. There are many superfamilies of Znf motifs, varying in both sequence and structure. They display considerable versatility in binding modes, even between members of the same class (e.g. some bind DNA, others protein), suggesting that Znf motifs are stable scaffolds that have evolved specialised functions. For example, Znf-containing proteins function in gene transcription, translation, mRNA trafficking, cytoskeleton organisation, epithelial development, cell adhesion, protein folding, chromatin remodelling and zinc sensing, to name but a few
[12]
. Zinc-binding motifs are stable structures, and they rarely undergo conformational changes upon binding their target.

This entry represents MYND-type zinc finger domains. The MYND domain (myeloid, Nervy, and DEAF-1) is present in a large group of proteins that includes RP-8 (PDCD2), Nervy, and predicted proteins from Drosophila, mammals, Caenorhabditis elegans, yeast, and plants
[10, 7, 11]
. The MYND domain consists of a cluster of cysteine and histidine residues, arranged with an invariant spacing to form a potential zinc-binding motif
[7]
. Mutating conserved cysteine residues in the DEAF-1 MYND domain does not abolish DNA binding, which suggests that the MYND domain might be involved in protein-protein interactions
[7]
. Indeed, the MYND domain of ETO/MTG8 interacts directly with the N-CoR and SMRT co-repressors
[9, 5]
. Aberrant recruitment of co-repressor complexes and inappropriate transcriptional repression is believed to be a general mechanism of leukaemogenesis caused by the t(8;21) translocations that fuse ETO with the acute myelogenous leukemia 1 (AML1) protein. ETO has been shown to be a co-repressor recruited by the promyelocytic leukaemia zinc finger (PLZF) protein
[6]
. A divergent MYND domain present in the adenovirus E1A binding protein BS69 was also shown to interact with N-CoR and mediate transcriptional repression
[4]
. The current evidence suggests that the MYND motif in mammalian proteins constitutes a protein-protein interaction domain that functions as a co-repressor-recruiting interface.

References
Imported from IPR002893

1.Zinc finger peptides for the regulation of gene expression. Klug A. J. Mol. Biol. 293, 215-8, (1999). View articlePMID: 10529348

2.Multiple modes of RNA recognition by zinc finger proteins. Hall TM. Curr. Opin. Struct. Biol. 15, 367-73, (2005). View articlePMID: 15963892

3.Zinc finger proteins: getting a grip on RNA. Brown RS. Curr. Opin. Struct. Biol. 15, 94-8, (2005). View articlePMID: 15718139

4.The adenovirus E1A binding protein BS69 is a corepressor of transcription through recruitment of N-CoR. Masselink H, Bernards R. Oncogene 19, 1538-46, (2000). View articlePMID: 10734313

5.ETO, a target of t(8;21) in acute leukemia, interacts with the N-CoR and mSin3 corepressors. Lutterbach B, Westendorf JJ, Linggi B, Patten A, Moniwa M, Davie JR, Huynh KD, Bardwell VJ, Lavinsky RM, Rosenfeld MG, Glass C, Seto E, Hiebert SW. Mol. Cell. Biol. 18, 7176-84, (1998). View articlePMID: 9819404

6.The ETO protein disrupted in t(8;21)-associated acute myeloid leukemia is a corepressor for the promyelocytic leukemia zinc finger protein. Melnick AM, Westendorf JJ, Polinger A, Carlile GW, Arai S, Ball HJ, Lutterbach B, Hiebert SW, Licht JD. Mol. Cell. Biol. 20, 2075-86, (2000). View articlePMID: 10688654

7.DEAF-1, a novel protein that binds an essential region in a Deformed response element. Gross CT, McGinnis W. EMBO J. 15, 1961-70, (1996). View articlePMID: 8617243

8.Sticky fingers: zinc-fingers as protein-recognition motifs. Gamsjaeger R, Liew CK, Loughlin FE, Crossley M, Mackay JP. Trends Biochem. Sci. 32, 63-70, (2007). View articlePMID: 17210253

9.The MYND motif is required for repression of basal transcription from the multidrug resistance 1 promoter by the t(8;21) fusion protein. Lutterbach B, Sun D, Schuetz J, Hiebert SW. Mol. Cell. Biol. 18, 3604-11, (1998). View articlePMID: 9584201

10.Identification of homeotic target genes in Drosophila melanogaster including nervy, a proto-oncogene homologue. Feinstein PG, Kornfeld K, Hogness DS, Mann RS. Genetics 140, 573-86, (1995). View articlePMID: 7498738

11.Identification of mRNAs associated with programmed cell death in immature thymocytes. Owens GP, Hahn WE, Cohen JJ. Mol. Cell. Biol. 11, 4177-88, (1991). View articlePMID: 2072913

12.Zinc finger proteins: new insights into structural and functional diversity. Laity JH, Lee BM, Wright PE. Curr. Opin. Struct. Biol. 11, 39-46, (2001). View articlePMID: 11179890

13.Zinc fingers--folds for many occasions. Matthews JM, Sunde M. IUBMB Life 54, 351-5, (2002). View articlePMID: 12665246

Wikipedia

This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our Privacy Notice and Terms of Use.