DSIF

DSIF (DRB Sensitivity Inducing Factor) is a protein complex that can either negatively or positively affect transcription by RNA polymerase II (Pol II).[1] It can interact with the negative elongation factor (NELF) to promote the stalling of Pol II at some genes. This stalling is relieved by P-TEFb.

In humans, DSIF is composed of hSPT4 and hSPT5 (SPT4 and SPT5 are homologs in yeast).[2] In bacteria, the homologous complex only contains NusG, a Spt5 homolog. Archaea have both proteins.[3]

The complex locks the RNA polymerase (RNAP) clamp into a closed state to prevent the elongation complex (EC) from dissociating. The Spt5 NGN domain helps anneal the two strands of DNA upstream. The single KOW domain in bacteria and archaea anchors a ribosome to the RNAP.[3]

References

  1. Wada T, Takagi T, Yamaguchi Y, Ferdous A, Imai T, Hirose S, et al. (February 1998). "DSIF, a novel transcription elongation factor that regulates RNA polymerase II processivity, is composed of human Spt4 and Spt5 homologs". Genes & Development. 12 (3): 343–356. doi:10.1101/gad.12.3.343. PMC 316480. PMID 9450929.
  2. Wenzel S, Schweimer K, Rösch P, Wöhrl BM (June 2008). "The small hSpt4 subunit of the human transcription elongation factor DSIF is a Zn-finger protein with alpha/beta type topology". Biochemical and Biophysical Research Communications. 370 (3): 414–418. doi:10.1016/j.bbrc.2008.03.080. PMID 18373978.
  3. Fouqueau T, Blombach F, Cackett G, Carty AE, Matelska DM, Ofer S, et al. (December 2018). "The cutting edge of archaeal transcription". Emerging Topics in Life Sciences. 2 (4): 517–533. doi:10.1042/ETLS20180014. PMC 7289017. PMID 33525828.
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