General information | DisProt: | DP00720 | Name: | FACT complex subunit Ssrp1 | Synonym(s): | SSRP1_DROME
Chorion-factor 5
Facilitates chromatin transcription complex subunit Ssrp1
Recombination signal sequence recognition protein
Single-strand recognition protein
dSSRP1
| First appeared in release: | Release 5.9 (02/23/2012) | UniProt: | Q05344 | UniGene: | | SwissProt: | SSRP1_DROME | TrEMBL: | | NCBI (GI): | | Source organism: | Drosophila melanogaster (Fruit fly) | Sequence length: | 723 | Percent disordered: | 100% | Homologues: | |
Native sequence |
10 20 30 40 50 60 | | | | | | MTDSLEYNDI NAEVRGVLCS GRLKMTEQNI IFKNTKTGKV EQISAEDIDL INSQKFVGTW - 60 GLRVFTKGGV LHRFTGFRDS EHEKLGKFIK AAYSQEMVEK EMCVKGWNWG TARFMGSVLS - 120 FDKESKTIFE VPLSHVSQCV TGKNEVTLEF HQNDDAPVGL LEMRFHIPAV ESAEEDPVDK - 180 FHQNVMSKAS VISASGESIA IFREIQILTP RGRYDIKIFS TFFQLHGKTF DYKIPMDSVL - 240 RLFMLPHKDS RQMFFVLSLD PPIKQGQTRY HYLVLLFAPD EETTIELPFS EAELRDKYEG - 300 KLEKEISGPV YEVMGKVMKV LIGRKITGPG NFIGHSGTAA VGCSFKAAAG YLYPLERGFI - 360 YIHKPPLHIR FEEISSVNFA RSGGSTRSFD FEVTLKNGTV HIFSSIEKEE YAKLFDYITQ - 420 KKLHVSNMGK DKSGYKDVDF GDSDNENEPD AYLARLKAEA REKEEDDDDG DSDEESTDED - 480 FKPNENESDV AEEYDSNVES DSDDDSDASG GGGDSDGAKK KKEKKSEKKE KKEKKHKEKE - 540 RTKKPSKKKK DSGKPKRATT AFMLWLNDTR ESIKRENPGI KVTEIAKKGG EMWKELKDKS - 600 KWEDAAAKDK QRYHDEMRNY KPEAGGDSDN EKGGKSSKKR KTEPSPSKKA NTSGSGFKSK - 660 EYISDDDSTS SDDEKDNEPA KKKSKPPSDG DAKKKKAKSE SEPEESEEDS NASDEDEEDE - 720 ASD
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Functional narrative |
Function: Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II. Binds specifically to single-stranded DNA and RNA with highest affinity for nucleotides G and U. The FACT complex is required for expression of Hox genes.
SUBUNIT: Component of the FACT complex, a stable heterodimer of dre4/spt16 and Ssrp. Interacts with CHD1 and TRL/GAGA.
Subcellular Location: Nucleus. Chromosome. Note=Colocalizes with RNA polymerase II on chromatin. Recruited to actively transcribed loci.
TISSUE SPECIFICITY: Expressed at highest levels in nurse cells of the ovary.
DEVELOPMENTAL STAGE: Abundant throughout oogenesis and embryogenesis, decreases during larval stages and increases again in pupae.
SIMILARITY: Belongs to the SSRP1 family.
SIMILARITY: Contains 1 HMG box DNA-binding domain. -----------------------------------------------------------------------
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Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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Region 1 | Type: | Disordered | Name: | N-terminal domain | Location: | 1 - 433 | Length: | 433 | Region sequence: |
MTDSLEYNDINAEVRGVLCSGRLKMTEQNIIFKNTKTGKVEQISAEDIDLINSQKFVGTW GLRVFTKGGVLHRFTGFRDSEHEKLGKFIKAAYSQEMVEKEMCVKGWNWGTARFMGSVLS FDKESKTIFEVPLSHVSQCVTGKNEVTLEFHQNDDAPVGLLEMRFHIPAVESAEEDPVDK FHQNVMSKASVISASGESIAIFREIQILTPRGRYDIKIFSTFFQLHGKTFDYKIPMDSVL RLFMLPHKDSRQMFFVLSLDPPIKQGQTRYHYLVLLFAPDEETTIELPFSEAELRDKYEG KLEKEISGPVYEVMGKVMKVLIGRKITGPGNFIGHSGTAAVGCSFKAAAGYLYPLERGFI YIHKPPLHIRFEEISSVNFARSGGSTRSFDFEVTLKNGTVHIFSSIEKEEYAKLFDYITQ KKLHVSNMGKDKS | Modification type: | Native
| PDB: | | Structural/functional type: | | Functional classes: | Molecular recognition effectors
| Functional subclasses: | Protein-DNA binding
| Detection methods:
- Atomic force microscopy (AFM) (pH: 7.5; FACT complex (FACT subunits SSRP1 and SPT16 in Buffer A) 2 uL; Buffer A (Tris-HCl, NaCl, glycerol, ME); Tris-HCl (Buffer B for AFM observation) 20 mM; MgCl2 (Buffer B for AFM observation) 10 mM; KCl (Buffer B for AFM observation) 50 mM)
| References:
- Miyagi A, Tsunaka Y, Uchihashi T, Mayanagi K, Hirose S, Morikawa K, Ando T. "Visualization of intrinsically disordered regions of proteins by high-speed atomic force microscopy." Chemphyschem. 2008; 9(13): 1859-66. PubMed: 18698566
- Tsunaka Y, Toga J, Yamaguchi H, Tate S, Hirose S, Morikawa K. "Phosphorylated intrinsically disordered region of FACT masks its nucleosomal DNA binding elements." J. Biol. Chem.. 2009; 284(36): 24610-21. PubMed: 19605348
| Comments:The N-terminal domain contains a structure-specific recognition (SSRC) motif at aa M186-K436.
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Region 2 | Type: | Disordered - Extended | Name: | IDR-Acidic | Location: | 434 - 518 | Length: | 85 | Region sequence: |
GYKDVDFGDSDNENEPDAYLARLKAEAREKEEDDDDGDSDEESTDEDFKPNENESDVAEE YDSNVESDSDDDSDASGGGGDSDGA | Modification type: | Complex
Native
| PDB: | | Structural/functional type: | Function arises from the disordered state | Functional classes: | Modification site
Molecular recognition effectors
| Functional subclasses: | Intraprotein interaction
Phosphorylation
Protein-protein binding
| Detection methods:
- Atomic force microscopy (AFM) (pH: 7.5; Buffer A (Tris-HCl, NaCl, glycerol, ME); FACT complex (FACT subunits SSRP1 and SPT16 in Buffer A) 2 uL; KCl (Buffer B for AFM observation) 50 mM; MgCl2 (Buffer B for AFM observation) 10 mM; Tris-HCl (Buffer B for AFM observation) 20 mM)
- Circular dichroism (CD) spectroscopy, far-UV (298 K; pH: 8.5; 2-mercaptoethanol 5 mM; dSSRP1 protein (Sf9-Mid-dSSRP1 (aa 186-624) ); NaCl 0.15 M; Tris-HCL 20 mM)
| References:
- Miyagi A, Tsunaka Y, Uchihashi T, Mayanagi K, Hirose S, Morikawa K, Ando T. "Visualization of intrinsically disordered regions of proteins by high-speed atomic force microscopy." Chemphyschem. 2008; 9(13): 1859-66. PubMed: 18698566
- Tsunaka Y, Toga J, Yamaguchi H, Tate S, Hirose S, Morikawa K. "Phosphorylated intrinsically disordered region of FACT masks its nucleosomal DNA binding elements." J. Biol. Chem.. 2009; 284(36): 24610-21. PubMed: 19605348
| Comments:Tsunaka et al (2009) describe that phosphorylation of the Acidic intrinsically disordered region (IDR) inhibits DNA binding of the HMG-box and Basic IDR regions.
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Region 3 | Type: | Disordered - Extended | Name: | IDR-Basic | Location: | 519 - 554 | Length: | 36 | Region sequence: |
KKKKEKKSEKKEKKEKKHKEKERTKKPSKKKKDSGK | Modification type: | Complex
Native
| PDB: | | Structural/functional type: | Function arises from the disordered state | Functional classes: | Modification site
Molecular recognition effectors
Molecular assembly
| Functional subclasses: | Intraprotein interaction
Phosphorylation
Protein-DNA binding
| Detection methods:
- Atomic force microscopy (AFM) (pH: 7.5; Buffer A (Tris-HCl, NaCl, glycerol, ME); FACT complex (FACT subunits SSRP1 and SPT16 in Buffer A) 2 uL; KCl (Buffer B for AFM observation) 50 mM; MgCl2 (Buffer B for AFM observation) 10 mM; Tris-HCl (Buffer B for AFM observation) 20 mM)
- Circular dichroism (CD) spectroscopy, far-UV (298 K; pH: 8.5; 2-mercaptoethanol 5 mM; dSSRP1 protein (Sf9-Mid-dSSRP1 (aa 186-624)); NaCl 0.15 M; Tris-HCL 20 mM)
| References:
- Miyagi A, Tsunaka Y, Uchihashi T, Mayanagi K, Hirose S, Morikawa K, Ando T. "Visualization of intrinsically disordered regions of proteins by high-speed atomic force microscopy." Chemphyschem. 2008; 9(13): 1859-66. PubMed: 18698566
- Tsunaka Y, Toga J, Yamaguchi H, Tate S, Hirose S, Morikawa K. "Phosphorylated intrinsically disordered region of FACT masks its nucleosomal DNA binding elements." J. Biol. Chem.. 2009; 284(36): 24610-21. PubMed: 19605348
| Comments:Tsunaka et al (2009) describe that phosphorylation of the Acidic intrinsically disordered region (IDR) inhibits DNA binding of the HMG-box and Basic IDR regions.
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Region 4 | Type: | Disordered | Name: | HMG-box domain | Location: | 555 - 624 | Length: | 70 | Region sequence: |
PKRATTAFMLWLNDTRESIKRENPGIKVTEIAKKGGEMWKELKDKSKWEDAAAKDKQRYH DEMRNYKPEA | Modification type: | Complex
Fragment
Native
| PDB: | 1WXL:A | Structural/functional type: | Function arises from the disordered state | Functional classes: | Molecular recognition effectors
Molecular assembly
| Functional subclasses: | Intraprotein interaction
Protein-DNA binding
| Detection methods:
- Atomic force microscopy (AFM) (pH: 7.5; Buffer A (Tris-HCl, NaCl, glycerol, ME); FACT complex (FACT subunits SSRP1 and SPT16 in Buffer A) 2 uL; KCl (Buffer B for AFM observation) 50 mM; MgCl2 (Buffer B for AFM observation) 10 mM; Tris-HCl (Buffer B for AFM observation) 20 mM)
- Nuclear magnetic resonance (NMR) (298 K; pH: 5.2; dFACT HMG domain (protein fragment) 2.2 mM; H2O/D2O (90%/10%, solvent); sodium acetate (buffer) 2 mM)
- Circular dichroism (CD) spectroscopy, far-UV (298 K; pH: 8.5; 2-mercaptoethanol 5 mM; dSSRP1 protein (Sf9-Mid-dSSRP1 (aa 186-624)); NaCl 0.15 M; Tris-HCl 20 mM)
| References:
- Kasai N, Tsunaka Y, Ohki I, Hirose S, Morikawa K, Tate S. "Solution structure of the HMG-box domain in the SSRP1 subunit of FACT." J. Biomol. NMR. 2005; 32(1): 83-8. PubMed: 16041486
- Miyagi A, Tsunaka Y, Uchihashi T, Mayanagi K, Hirose S, Morikawa K, Ando T. "Visualization of intrinsically disordered regions of proteins by high-speed atomic force microscopy." Chemphyschem. 2008; 9(13): 1859-66. PubMed: 18698566
- Tsunaka Y, Toga J, Yamaguchi H, Tate S, Hirose S, Morikawa K. "Phosphorylated intrinsically disordered region of FACT masks its nucleosomal DNA binding elements." J. Biol. Chem.. 2009; 284(36): 24610-21. PubMed: 19605348
| Comments:PDB structure 1WXL, from Kasai et al (2005), was characterized using protein fragment comprising the HMG-box domain, aa P555-A624.
Secondary structure of HMG-box domain consists of three alpha-helices at A561-R575, V582-K594 and S600-R618 connected by loops at E576-K581 and E595-K599.
Tsunaka et al (2009) describe that phosphorylation of the Acidic intrinsically disordered region (IDR) inhibits DNA binding of the HMG-box and Basic IDR regions.
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Region 5 | Type: | Disordered - Extended | Name: | IDR-Mixed | Location: | 625 - 723 | Length: | 99 | Region sequence: |
GGDSDNEKGGKSSKKRKTEPSPSKKANTSGSGFKSKEYISDDDSTSSDDEKDNEPAKKKS KPPSDGDAKKKKAKSESEPEESEEDSNASDEDEEDEASD | Modification type: | Native
| PDB: | | Structural/functional type: | Function arises from the disordered state | Functional classes: | Modification site
Molecular recognition effectors
| Functional subclasses: | Intraprotein interaction
Phosphorylation
| Detection methods:
- Atomic force microscopy (AFM) (pH: 7.5; Buffer A (Tris-HCl, NaCl, glycerol, ME); FACT complex (FACT subunits SSRP1 and SPT16 in Buffer A) 2 uL; KCl (Buffer B for AFM observation) 50 mM; MgCl2 (Buffer B for AFM observation) 10 mM; Tris-HCl (Buffer B for AFM observation) 20 mM)
| References:
- Miyagi A, Tsunaka Y, Uchihashi T, Mayanagi K, Hirose S, Morikawa K, Ando T. "Visualization of intrinsically disordered regions of proteins by high-speed atomic force microscopy." Chemphyschem. 2008; 9(13): 1859-66. PubMed: 18698566
- Tsunaka Y, Toga J, Yamaguchi H, Tate S, Hirose S, Morikawa K. "Phosphorylated intrinsically disordered region of FACT masks its nucleosomal DNA binding elements." J. Biol. Chem.. 2009; 284(36): 24610-21. PubMed: 19605348
| Comments:The IDR-Mixed region consists of interspersed basic and acidic segments. It also contains phosphorylation sites, but these were not involved in the DNA-binding inhibitory effect found with the Acidic IDR (Tsunaka 2009).
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References |
- Fuxreiter M, Simon I, Bondos S. "Dynamic protein-DNA recognition: beyond what can be seen." Trends Biochem. Sci.. 2011; 36(8): 415-23. PubMed: 21620710
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Comments |
A discussion of the dynamic nature and competitive binding of FACT in a "fuzzy" protein-DNA complex is found in Fuxreiter et al (2011).
Verification request sent 2-22-2012 (PMID: 18698566)
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