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SUPT16H  -  suppressor of Ty 16 homolog (S. cerevisiae)

Homo sapiens

Synonyms: CDC68, Chromatin-specific transcription elongation factor 140 kDa subunit, FACT, FACT 140 kDa subunit, FACT complex subunit SPT16, ...
 
 
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High impact information on SUPT16H

  • Over-expression of ySpt16p/Cdc68p suppressed the phenotype of cold sensitivity of the yTFIIE-alpha-cs mutant strain, and in vitro binding assays revealed that yTFIIE-alpha-cs mutant protein showed diminished binding affinity to ySpt16p/Cdc68p [1].
Role of SUPT16H in transcription
  • SUPT16H interacts with SSRP1 and cooperates with monoubiquitinated histone H2B (by RNF20 and RNF40) during transcriptional elongation [2].
  • SUPT16H and SSRP1 make up the Facilitates Chromatin Transcription (FACT) histone chaperone complex [3].
  • The SUPT16H and SSRP1-containing FACT histone chaperone complex functions to increase transcription by opening chromatin through the displacement of an H2A-H2B dimer from the nucleosome octamer [4].

Role of SUPT16H in DNA repair

  • SUPT16H recognizes the phosphorylated histone variant H2AX (γH2AX) and catalyzes the exchange of an H2AX-H2B dimer in vitro [5].
  • SUPT16H histone chaperone activity is regulated by ADP-ribosylation [5] [6].

References

  1. Functional interaction of general transcription initiation factor TFIIE with general chromatin factor SPT16/CDC68. Kang, S.W., Kuzuhara, T., Horikoshi, M. Genes Cells (2000) [Pubmed]
  2. Histone H2B monoubiquitination functions cooperatively with FACT to regulate elongation by RNA polymerase II. Pavri, R., Zhu, B., Li, G., Trojer, P., Mandal, S., Shilatifard, A., Reinberg, D. Cell. (2006) [Pubmed]
  3. The chromatin-specific transcription elongation factor FACT comprises human SPT16 and SSRP1 proteins. Orphanides, G., Wu, W.H., Lane, W.S., Hampsey, M., Reinberg, D. Nature. (1999) [Pubmed]
  4. FACT facilitates transcription-dependent nucleosome alteration. Belotserkovskaya, R., Oh, S., Bondarenko, V.A., Orphanides, G., Studitsky, V.M., Reinberg, D. Science. (2003) [Pubmed]
  5. FACT-mediated exchange of histone variant H2AX regulated by phosphorylation of H2AX and ADP-ribosylation of Spt16. Heo, K., Kim, H., Choi, S.H., Choi, J., Kim, K., Gu, J., Lieber, M.R., Yang, A.S., An, W. Mol. Cell. (2008) [Pubmed]
  6. Modulation of nucleosome-binding activity of FACT by poly(ADP-ribosyl)ation. Huang, J.Y., Chen, W.H., Chang, Y.L., Wang, H.T., Chuang, W.T., Lee, S.C. Nucleic. Acids. Res. (2006) [Pubmed]
 
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