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PDBsum entry 2mpl
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Transcription
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PDB id
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2mpl
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PDB id:
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Transcription
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Title:
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Solution structure of the pr domain of fog-1
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Structure:
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Zinc finger protein zfpm1. Chain: a. Synonym: friend of gata protein 1, fog-1, friend of gata 1, zinc finger protein multitype 1. Engineered: yes
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Source:
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Mus musculus. Mouse. Organism_taxid: 10090. Gene: fog, fog1, zfpm1. Expressed in: escherichia coli. Expression_system_taxid: 511693.
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NMR struc:
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20 models
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Authors:
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J.P.Mackay,M.K.Clifton,B.J.Westman,G.A.Blobel
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Key ref:
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M.K.Clifton
et al.
(2014).
The identification and structure of an N-terminal PR domain show that FOG1 is a member of the PRDM family of proteins.
Plos One,
9,
e106011.
PubMed id:
DOI:
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Date:
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26-May-14
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Release date:
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29-Oct-14
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PROCHECK
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Headers
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References
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O35615
(FOG1_MOUSE) -
Zinc finger protein ZFPM1 from Mus musculus
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Seq:
Struc:
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995 a.a.
127 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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DOI no:
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Plos One
9:e106011
(2014)
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PubMed id:
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The identification and structure of an N-terminal PR domain show that FOG1 is a member of the PRDM family of proteins.
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M.K.Clifton,
B.J.Westman,
S.Y.Thong,
M.R.O'Connell,
M.W.Webster,
N.E.Shepherd,
K.G.Quinlan,
M.Crossley,
G.A.Blobel,
J.P.Mackay.
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ABSTRACT
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FOG1 is a transcriptional regulator that acts in concert with the hematopoietic
master regulator GATA1 to coordinate the differentiation of platelets and
erythrocytes. Despite considerable effort, however, the mechanisms through which
FOG1 regulates gene expression are only partially understood. Here we report the
discovery of a previously unrecognized domain in FOG1: a PR (PRD-BF1 and RIZ)
domain that is distantly related in sequence to the SET domains that are found
in many histone methyltransferases. We have used NMR spectroscopy to determine
the solution structure of this domain, revealing that the domain shares close
structural similarity with SET domains. Titration with
S-adenosyl-L-homocysteine, the cofactor product synonymous with SET domain
methyltransferase activity, indicated that the FOG PR domain is not, however,
likely to function as a methyltransferase in the same fashion. We also sought to
define the function of this domain using both pulldown experiments and gel shift
assays. However, neither pulldowns from mammalian nuclear extracts nor yeast
two-hybrid assays reproducibly revealed binding partners, and we were unable to
detect nucleic-acid-binding activity in this domain using our high-diversity
Pentaprobe oligonucleotides. Overall, our data demonstrate that FOG1 is a member
of the PRDM (PR domain containing proteins, with zinc fingers) family of
transcriptional regulators. The function of many PR domains, however, remains
somewhat enigmatic for the time being.
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Links
