DSIF complex binds to RNA Pol II (hypophosphorylated)

Stable Identifier
Reaction [binding]
Homo sapiens
Related Species
Human immunodeficiency virus 1
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This HIV-1 event was inferred from the corresponding human RNA Pol II transcription event. DSIF is a heterodimer consisting of hSPT4 (human homolog of yeast Spt4- p14) and hSPT5 (human homolog of yeast Spt5-p160) (Wada et al. 1998). DSIF association with Pol II may be enabled by Spt5 binding to Pol II creating a scaffold for NELF binding. Spt5 subunit of DSIF can be phosphorylated by P-TEFb (Ivanov et al. 2000).
Literature References
PubMed ID Title Journal Year
10757782 Domains in the SPT5 protein that modulate its transcriptional regulatory properties

Gaynor, RB, Kwak, YT, Ivanov, D, Guo, J

Mol Cell Biol 2000
9857195 Evidence that P-TEFb alleviates the negative effect of DSIF on RNA polymerase II-dependent transcription in vitro.

Takagi, T, Wada, T, Handa, H, Watanabe, D, Yamaguchi, Y

EMBO J 1999
9450929 DSIF, a novel transcription elongation factor that regulates RNA polymerase II processivity, is composed of human Spt4 and Spt5 homologs.

Takagi, T, Buratowski, S, Yano, K, Ferdous, A, Wada, T, Handa, H, Winston, F, Yamaguchi, Y, Sugimoto, S, Hartzog, GA, Imai, T, Hirose, S

Genes Dev 1998
12653964 Structure-function analysis of human Spt4: evidence that hSpt4 and hSpt5 exert their roles in transcriptional elongation as parts of the DSIF complex.

Furuya, A, Sato, H, Kim, DK, Yamada, T, Wada, T, Handa, H, Inukai, N, Yamaguchi, Y

Genes Cells 2003
Inferred From
Name Identifier Synonyms
Human immunodeficiency virus infectious disease DOID:526 HIV infection
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