FACT complex subunit POB3 - Saccharomyces cerevisiae (Baker's yeast)

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Reviewed, UniProtKB/Swiss-Prot Q04636 (POB3_YEAST)

Last modified September 2, 2008. Version 62. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
FACT complex subunit POB3
Alternative name(s):
Facilitates chromatin transcription complex subunit POB3

Gene names

Name:	POB3
Ordered Locus Names:	YML069W

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length	552 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

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 reestablishement of the nucleosome following the passage of RNA polymerase II. Transcription elongation is promoted by the repression of transcription initiation from cryptic sites. Also acts in establishing transcription initiation complexes and promotes SPT15/TBP-binding to a TATA box. Together with replication factor-A protein (RPA), FACT may play a role in nucleosome deposition during DNA replication.
Subunit structure	Forms a stable heterodimer with SPT16. The SPT16-POB3 dimer weakly associates with multiple molecules of NHP6 (NHP6A or NHP6B) to form the FACT (yFACT or SNP) complex. The FACT complex interacts with the CK2 (casein kinase II) complex subunits CKA1, CKA2, CKB1 and CKB2 and the components of the transcription machinery CHD1, CTR9, PAF1 and CDC73. The FACT complex interacts with the PAF1 complex. SPT16 interacts with SAS3 and POL1. Interacts directly with RFA1.
Subcellular location	Nucleus. Note= Colocalizes with RNA polymerase II on chromatin. Recruited to actively transcribed loci.
Miscellaneous	In contrast to the orthologous protein in animals and plants, this protein does not contain a HMG box DNA-binding domain. This function may instead be provided by the HMG box of the associated NHP6A/NHP6B proteins in the FACT complex of yeast. Present with 22400 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the SSRP1 family.

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Ontologies

Keywords
Biological process	DNA damage DNA repair DNA replication Transcription Transcription regulation
Cellular component	Chromosomal protein Nucleus
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	DNA-dependent DNA replication Ref.2 Inferred from physical interaction. Source: SGD RNA elongation from RNA polymerase II promoter Ref.4 Inferred from physical interaction. Source: SGD nucleosome assembly Ref.14 Ref.20 Inferred from direct assay. Source: SGD transcription initiation from RNA polymerase II promoter Ref.21 Inferred from direct assay. Source: SGD
Cellular component	FACT complex Ref.4 Ref.8 Inferred from direct assay. Source: SGD nuclear chromatin Ref.5 Inferred from direct assay. Source: SGD
Molecular function	chromatin binding Ref.5 Inferred from direct assay. Source: SGD protein binding Ref.12 Ref.25 Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
RFA1	P22336	2	EBI-27863,EBI-14971
SPT16	P32558	1	EBI-27863,EBI-4334

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Chain

1 – 552

552

FACT complex subunit POB3

Amino acid modifications

Modified residue

194

Phosphoserine

Modified residue

195

Phosphoserine

Experimental info

Mutagenesis

R → H in pob3-11; causes severe defects in rate of growth; when associated with C-109

Mutagenesis

L → R in pob3-1; causes severe defects in rate of growth; when associated with K-419 and T-489

Mutagenesis

109

R → C in pob3-11; causes severe defects in rate of growth; when associated with H-20

Mutagenesis

308

Q → A or D: No effect

Mutagenesis

308

Q → K: Confers sensitivity to HU indicating a disturbed activity in DNA replication; confers a SPT- phenotype indicating a disturbed activity in transcription

Mutagenesis

308

Q → R: Confers sensitivity to HU indicating a disturbed activity in DNA replication

Mutagenesis

311

T → A: No change of sensitivity to HU; confers a SPT- phenotype indicating a disturbed activity in transcription

Mutagenesis

419

M → K in pob3-1; causes severe defects in rate of growth; when associated with R-78 and T-489

Mutagenesis

489

S → T in pob3-1; causes severe defects in rate of growth; when associated with R-78 and K-419

Mutagenesis

547

K → M in pob3-21; causes severe defects in rate of growth

Secondary structure

552

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

Q04636-1 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 02C04F620C7B1450
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FASTA

552

62,994

        10         20         30         40         50         60 
MSTDFDRIYL NQSKFSGRFR IADSGLGWKI STSGGSAANQ ARKPFLLPAT ELSTVQWSRG 

        70         80         90        100        110        120 
CRGYDLKINT KNQGVIQLDG FSQDDYNLIK NDFHRRFNIQ VEQREHSLRG WNWGKTDLAR 

       130        140        150        160        170        180 
NEMVFALNGK PTFEIPYARI NNTNLTSKNE VGIEFNIQDE EYQPAGDELV EMRFYIPGVI 

       190        200        210        220        230        240 
QTNVDENMTK KEESSNEVVP KKEDGAEGED VQMAVEEKSM AEAFYEELKE KADIGEVAGD 

       250        260        270        280        290        300 
AIVSFQDVFF TTPRGRYDID IYKNSIRLRG KTYEYKLQHR QIQRIVSLPK ADDIHHLLVL 

       310        320        330        340        350        360 
AIEPPLRQGQ TTYPFLVLQF QKDEETEVQL NLEDEDYEEN YKDKLKKQYD AKTHIVLSHV 

       370        380        390        400        410        420 
LKGLTDRRVI VPGEYKSKYD QCAVSCSFKA NEGYLYPLDN AFFFLTKPTL YIPFSDVSMV 

       430        440        450        460        470        480 
NISRAGQTST SSRTFDLEVV LRSNRGSTTF ANISKEEQQL LEQFLKSKNL RVKNEDREVQ 

       490        500        510        520        530        540 
ERLQTALGSD SDEEDINMGS AGEDDESVDE DFQVSSDNDA DEVAEEFDSD AALSDAEGGS 

       550 
DEERPSKKPK VE

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. Barrell B.G. Nature 387:90-93(1997) [PubMed: 9169872] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	"The Saccharomyces cerevisiae DNA polymerase alpha catalytic subunit interacts with Cdc68/Spt16 and with Pob3, a protein similar to an HMG1-like protein." Wittmeyer J., Formosa T. Mol. Cell. Biol. 17:4178-4190(1997) [PubMed: 9199353] [Abstract] Cited for: INTERACTION WITH POL1.
[3]	"The yeast protein complex containing cdc68 and pob3 mediates core-promoter repression through the cdc68 N-terminal domain." Evans D.R.H., Brewster N.K., Xu Q., Rowley A., Altheim B.A., Johnston G.C., Singer R.A. Genetics 150:1393-1405(1998) [PubMed: 9832518] [Abstract] Cited for: INTERACTION WITH SPT16.
[4]	"Characterization of the CP complex, an abundant dimer of Cdc68 and Pob3 proteins that regulates yeast transcriptional activation and chromatin repression." Brewster N.K., Johnston G.C., Singer R.A. J. Biol. Chem. 273:21972-21979(1998) [PubMed: 9705338] [Abstract] Cited for: INTERACTION WITH SPT16.
[5]	"Spt16 and Pob3 of Saccharomyces cerevisiae form an essential, abundant heterodimer that is nuclear, chromatin-associated, and copurifies with DNA polymerase alpha." Wittmeyer J., Joss L., Formosa T. Biochemistry 38:8961-8971(1999) [PubMed: 10413469] [Abstract] Cited for: FUNCTION, INTERACTION WITH SPT16, SUBCELLULAR LOCATION.
[6]	"The something about silencing protein, Sas3, is the catalytic subunit of NuA3, a yTAF(II)30-containing HAT complex that interacts with the Spt16 subunit of the yeast CP (Cdc68/Pob3)-FACT complex." John S., Howe L., Tafrov S.T., Grant P.A., Sternglanz R., Workman J.L. Genes Dev. 14:1196-1208(2000) [PubMed: 10817755] [Abstract] Cited for: INTERACTION WITH SAS3.
[7]	"POB3 is required for both transcription and replication in the yeast Saccharomyces cerevisiae." Schlesinger M.B., Formosa T. Genetics 155:1593-1606(2000) [PubMed: 10924459] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF ARG-20; LEU-78; ARG-109; MET-419; SER-489 AND LYS-547.
[8]	"Spt16-Pob3 and the HMG protein Nhp6 combine to form the nucleosome-binding factor SPN." Formosa T., Eriksson P., Wittmeyer J., Ginn J., Yu Y., Stillman D.J. EMBO J. 20:3506-3517(2001) [PubMed: 11432837] [Abstract] Cited for: ASSOCIATION OF THE SPT16-POB3 DIMER WITH NHP6A/B AND NUCLEOSOMES, FUNCTION OF THE FACT COMPLEX.
[9]	"A bipartite yeast SSRP1 analog comprised of Pob3 and Nhp6 proteins modulates transcription." Brewster N.K., Johnston G.C., Singer R.A. Mol. Cell. Biol. 21:3491-3502(2001) [PubMed: 11313475] [Abstract] Cited for: ASSOCIATION OF THE SPT16-POB3 DIMER WITH NHP6A/B.
[10]	"The Paf1 complex physically and functionally associates with transcription elongation factors in vivo." Squazzo S.L., Costa P.J., Lindstrom D.L., Kumer K.E., Simic R., Jennings J.L., Link A.J., Arndt K.M., Hartzog G.A. EMBO J. 21:1764-1774(2002) [PubMed: 11927560] [Abstract] Cited for: INTERACTION WITH PAF1 COMPLEX.
[11]	"Defects in SPT16 or POB3 (yFACT) in Saccharomyces cerevisiae cause dependence on the Hir/Hpc pathway: polymerase passage may degrade chromatin structure." Formosa T., Ruone S., Adams M.D., Olsen A.E., Eriksson P., Yu Y., Rhoades A.R., Kaufman P.D., Stillman D.J. Genetics 162:1557-1571(2002) [PubMed: 12524332] [Abstract] Cited for: FUNCTION OF THE FACT COMPLEX.
[12]	"RNA polymerase II elongation factors of Saccharomyces cerevisiae: a targeted proteomics approach." Krogan N.J., Kim M., Ahn S.H., Zhong G., Kobor M.S., Cagney G., Emili A., Shilatifard A., Buratowski S., Greenblatt J.F. Mol. Cell. Biol. 22:6979-6992(2002) [PubMed: 12242279] [Abstract] Cited for: INTERACTION WITH CHD1; CTR9; PAF1; CDC73; CKA1; CKA2; CKB1; CKB2 AND HISTONES.
[13]	"Chromatin remodeling protein Chd1 interacts with transcription elongation factors and localizes to transcribed genes." Simic R., Lindstrom D.L., Tran H.G., Roinick K.L., Costa P.J., Johnson A.D., Hartzog G.A., Arndt K.M. EMBO J. 22:1846-1856(2003) [PubMed: 12682017] [Abstract] Cited for: INTERACTION WITH CHD1.
[14]	"Multiple Nhp6 molecules are required to recruit Spt16-Pob3 to form yFACT complexes and to reorganize nucleosomes." Ruone S., Rhoades A.R., Formosa T. J. Biol. Chem. 278:45288-45295(2003) [PubMed: 12952948] [Abstract] Cited for: ASSOCIATION OF THE SPT16-POB3 DIMER WITH NHP6A/B.
[15]	"The FACT complex travels with elongating RNA polymerase II and is important for the fidelity of transcriptional initiation in vivo." Mason P.B., Struhl K. Mol. Cell. Biol. 23:8323-8333(2003) [PubMed: 14585989] [Abstract] Cited for: FUNCTION OF THE FACT COMPLEX, SUBCELLULAR LOCATION.
[16]	Erratum Mason P.B., Struhl K. Mol. Cell. Biol. 24:6536-6536(2004)
[17]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[18]	"Transcription elongation factors repress transcription initiation from cryptic sites." Kaplan C.D., Laprade L., Winston F. Science 301:1096-1099(2003) [PubMed: 12934008] [Abstract] Cited for: FUNCTION OF THE FACT COMPLEX.
[19]	"Transitions in RNA polymerase II elongation complexes at the 3' ends of genes." Kim M., Ahn S.-H., Krogan N.J., Greenblatt J.F., Buratowski S. EMBO J. 23:354-364(2004) [PubMed: 14739930] [Abstract] Cited for: SUBCELLULAR LOCATION.
[20]	"Structural features of nucleosomes reorganized by yeast FACT and its HMG box component, Nhp6." Rhoades A.R., Ruone S., Formosa T. Mol. Cell. Biol. 24:3907-3917(2004) [PubMed: 15082784] [Abstract] Cited for: FUNCTION OF THE FACT COMPLEX.
[21]	"The yeast FACT complex has a role in transcriptional initiation." Biswas D., Yu Y., Prall M., Formosa T., Stillman D.J. Mol. Cell. Biol. 25:5812-5822(2005) [PubMed: 15987999] [Abstract] Cited for: FUNCTION OF THE FACT COMPLEX.
[22]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194 AND SER-195, MASS SPECTROMETRY.
[23]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194 AND SER-195, MASS SPECTROMETRY.
[24]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194 AND SER-195, MASS SPECTROMETRY.
[25]	"The structure of the yFACT Pob3-M domain, its interaction with the DNA replication factor RPA, and a potential role in nucleosome deposition." Vandemark A.P., Blanksma M., Ferris E., Heroux A., Hill C.P., Formosa T. Mol. Cell 22:363-374(2006) [PubMed: 16678108] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 220-478, FUNCTION, INTERACTION WITH RFA1, MUTAGENESIS OF GLN-308 AND THR-311.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

Z38114 Genomic DNA. Translation: CAA86251.1.

PIR

S48328.

RefSeq

NP_013642.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2GCJ	X-ray	2.55	A/B/C/D	220-478	[»]
2GCL	X-ray	2.21	A/B	220-478	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:4083N.

IntAct

Q04636.

Proteomic databases

PeptideAtlas

Q04636.

Genome annotation databases

Ensembl

YML069W. Saccharomyces cerevisiae. [Contig view]

GeneID

854933.

GenomeReviews

Gene locus YML069W in contig Z71257_GR.

KEGG

sce:YML069W.

NMPDR

fig|4932.3.peg.4679.

Organism-specific databases

CYGD

YML069w.

SGD

S000004534. POB3.

Yeast-GFP

Search...

Phylogenomic databases

HOGENOM

Q04636.

Gene expression databases

GermOnline

YML069W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR000969. SSrcognition.
[Graphical view]

Pfam

PF03531. SSrecog. 1 hit.
[Graphical view]

PRINTS

PR00887. SSRCOGNITION.

ProDom

Q04636.
[Graphical view] [Entries sharing at least one domain]

BLOCKS

Search...

Other Resources

LinkHub

Q04636.

ProtoNet

Search...

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Entry information

Entry name

POB3_YEAST

Accession

Primary (citable) accession number: Q04636

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	September 2, 2008
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome XIII

Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents