1fv5

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SOLUTION STRUCTURE OF THE FIRST ZINC FINGER FROM THE DROSOPHILA U-SHAPED TRANSCRIPTION FACTOR

Structural highlights

1fv5 is a 1 chain structure with sequence from Drosophila melanogaster. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Ligands:ZN
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

USH_DROME Transcription regulator that modulates expression mediated by transcription factors of the GATA family such as pnr and srp. Represses transcription of proneural achaete-scute complex (AS-C), which is usually activated by pnr. Involved in cardiogenesis, blood, and eye development. During hematopoiesis, it is required to restrict the number of crystal cells, probably via its interaction with the isoform SrpNC of srp. Negatively regulates expression of sr. Probably acts by interacting with the GATA-type zinc finger of proteins such as pnr and srp, possibly antagonizing the interaction between the GATA-type zinc finger and some cofactor.[1] [2] [3] [4] [5] [6]

Publication Abstract from PubMed

BACKGROUND: Zinc finger domains have traditionally been regarded as sequence-specific DNA binding motifs. However, recent evidence indicates that many zinc fingers mediate specific protein-protein interactions. For instance, several zinc fingers from FOG family proteins have been shown to interact with the N-terminal zinc finger of GATA-1. RESULTS: We have used NMR spectroscopy to determine the first structures of two FOG family zinc fingers that are involved in protein-protein interactions: fingers 1 and 9 from U-shaped. These fingers resemble classical TFIIIA-like zinc fingers, with the exception of an unusual extended portion of the polypeptide backbone prior to the fourth zinc ligand. [15N,(1)H]-HSQC titrations have been used to define the GATA binding surface of USH-F1, and comparison with other FOG family proteins indicates that the recognition mechanism is conserved across species. The surface of FOG-type fingers that interacts with GATA-1 overlaps substantially with the surface through which classical fingers typically recognize DNA. This suggests that these fingers could not contact both GATA and DNA simultaneously. In addition, results from NMR, gel filtration, and sedimentation equilibrium experiments suggest that the interactions are of moderate affinity. CONCLUSIONS: Our results demonstrate unequivocally that zinc fingers comprising the classical betabetaalpha fold are capable of mediating specific contacts between proteins. The existence of this alternative function has implications for the prediction of protein function from sequence data and for the evolution of protein function.

Solution structures of two CCHC zinc fingers from the FOG family protein U-shaped that mediate protein-protein interactions.,Liew CK, Kowalski K, Fox AH, Newton A, Sharpe BK, Crossley M, Mackay JP Structure. 2000 Nov 15;8(11):1157-66. PMID:11080638[7]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
5 reviews cite this structure
Zinc finger proteins: new insights into structural and functional diversity.
Laity et al. (2001)
4 more
18 other articles
No citations found

References

  1. ↑ Cubadda Y, Heitzler P, Ray RP, Bourouis M, Ramain P, Gelbart W, Simpson P, Haenlin M. u-shaped encodes a zinc finger protein that regulates the proneural genes achaete and scute during the formation of bristles in Drosophila. Genes Dev. 1997 Nov 15;11(22):3083-95. PMID:9367989
  2. ↑ Haenlin M, Cubadda Y, Blondeau F, Heitzler P, Lutz Y, Simpson P, Ramain P. Transcriptional activity of pannier is regulated negatively by heterodimerization of the GATA DNA-binding domain with a cofactor encoded by the u-shaped gene of Drosophila. Genes Dev. 1997 Nov 15;11(22):3096-108. PMID:9367990
  3. ↑ Fossett N, Zhang Q, Gajewski K, Choi CY, Kim Y, Schulz RA. The multitype zinc-finger protein U-shaped functions in heart cell specification in the Drosophila embryo. Proc Natl Acad Sci U S A. 2000 Jun 20;97(13):7348-53. PMID:10861002
  4. ↑ Fossett N, Tevosian SG, Gajewski K, Zhang Q, Orkin SH, Schulz RA. The Friend of GATA proteins U-shaped, FOG-1, and FOG-2 function as negative regulators of blood, heart, and eye development in Drosophila. Proc Natl Acad Sci U S A. 2001 Jun 19;98(13):7342-7. Epub 2001 Jun 12. PMID:11404479 doi:http://dx.doi.org/10.1073/pnas.131215798
  5. ↑ Waltzer L, Bataille L, Peyrefitte S, Haenlin M. Two isoforms of Serpent containing either one or two GATA zinc fingers have different roles in Drosophila haematopoiesis. EMBO J. 2002 Oct 15;21(20):5477-86. PMID:12374748
  6. ↑ Ghazi A, Paul L, VijayRaghavan K. Prepattern genes and signaling molecules regulate stripe expression to specify Drosophila flight muscle attachment sites. Mech Dev. 2003 May;120(5):519-28. PMID:12782269
  7. ↑ Liew CK, Kowalski K, Fox AH, Newton A, Sharpe BK, Crossley M, Mackay JP. Solution structures of two CCHC zinc fingers from the FOG family protein U-shaped that mediate protein-protein interactions. Structure. 2000 Nov 15;8(11):1157-66. PMID:11080638

Contents


PDB ID 1fv5

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