GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.

Have any questions? Please email us at ecoliwiki@gmail.com

PMID:19605348

From GONUTS
Jump to: navigation, search
Citation

Tsunaka, Y, Toga, J, Yamaguchi, H, Tate, S, Hirose, S and Morikawa, K (2009) Phosphorylated intrinsically disordered region of FACT masks its nucleosomal DNA binding elements. J. Biol. Chem. 284:24610-21

Abstract

FACT is a heterodimer of SPT16 and SSRP1, which each contain several conserved regions in the primary structure. The interaction of FACT with nucleosomes induces chromatin remodeling through the combinatorial action of its distinct functional protein regions. However, there is little mechanistic insight into how these regions cooperatively contribute to FACT functions, particularly regarding the recognition of nucleosomal DNA. Here, we report the identification of novel phosphorylation sites of Drosophila melanogaster FACT (dFACT) expressed in Sf9 cells. These sites are densely concentrated in the acidic intrinsically disordered (ID) region of the SSRP1 subunit and control nucleosomal DNA binding by dFACT. This region and the adjacent segment of the HMG domain form weak electrostatic intramolecular interactions, which is reinforced by the phosphorylation, thereby blocking DNA binding competitively. Importantly, this control mechanism appears to support rapid chromatin transactions during early embryogenesis through the dephosphorylation of some sites in the maternally transmitted dSSRP1.

Links

PubMed PMC2782050 Online version:10.1074/jbc.M109.001958

Keywords

Animals; Carrier Proteins/genetics; Carrier Proteins/metabolism; Chromatin Assembly and Disassembly/physiology; DNA/genetics; DNA/metabolism; DNA-Binding Proteins/genetics; DNA-Binding Proteins/metabolism; Drosophila Proteins/genetics; Drosophila Proteins/metabolism; Drosophila melanogaster; Embryo, Nonmammalian/metabolism; Embryonic Development/physiology; High Mobility Group Proteins/genetics; High Mobility Group Proteins/metabolism; Nucleosomes/genetics; Nucleosomes/metabolism; Phosphorylation/physiology; Protein Structure, Tertiary/physiology; Transcriptional Elongation Factors/genetics; Transcriptional Elongation Factors/metabolism

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

DROME:SSRP1

enables

GO:0031492: nucleosomal DNA binding

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

DROME:SSRP1

enables

GO:0043621: protein self-association

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

DROME:SSRP1

part_of

GO:0035101: FACT complex

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

DROME:SSRP1

involved_in

GO:0051101: regulation of DNA binding

ECO:0000315: mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

DROME:SSRP1

located_in

GO:0005634: nucleus

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

DROME:SSRP1

located_in

GO:0005829: cytosol

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

DROME:SSRP1

enables

GO:0046982: protein heterodimerization activity

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q8IRG6

F

Seeded From UniProt

complete

DROME:SPT16

part_of

GO:0035101: FACT complex

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

DROME:SPT16

located_in

GO:0005829: cytosol

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

DROME:SPT16

enables

GO:0046982: protein heterodimerization activity

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q05344

F

Seeded From UniProt

complete


See also

References

See Help:References for how to manage references in GONUTS.