IPR022800
Spt4/RpoE2 zinc finger
InterPro entry
Short name | Spt4/RpoE2_Znf |
Overlapping homologous superfamilies |
Description
This entry consists of several eukaryotic transcription elongation Spt4 proteins as well as archaebacterial RpoE2
[1]. Three transcription-elongation factors Spt4, Spt5, and Spt6 are conserved among eukaryotes and are essential for transcription via the modulation of chromatin structure. Spt4 and Spt5 are tightly associated in a complex, while the physical association of the Spt4-Spt5 complex with Spt6 is considerably weaker. It has been demonstrated that Spt4, Spt5, and Spt6 play roles in transcription elongation in both yeast and humans including a role in activation by Tat. It is known that Spt4, Spt5, and Spt6 are general transcription-elongation factors, controlling transcription both positively and negatively in important regulatory and developmental roles
[2]. RpoE2 is one of 13 subunits in the archaeal RNA polymerase. These proteins contain a C4-type zinc finger, and the structure has been solved in
[3]. The structure reveals that Spt4-Spt5 binding is governed by an acid-dipole interaction between Spt5 and Spt4, and the complex binds to and travels along the elongating RNA polymerase. The Spt4-Spt5 complex is likely to be an ancient, core component of the transcription elongation machinery.
References
1.A subunit of an archaeal DNA-dependent RNA polymerase contains the S1 motif. Langer D, Lottspeich F, Zillig W. Nucleic Acids Res. 22, 694, (1994). View articlePMID: 8127719
2.Control of eukaryotic transcription elongation. Winston F. Genome Biol. 2, REVIEWS1006, (2001). View articlePMID: 11182892
3.Core structure of the yeast spt4-spt5 complex: a conserved module for regulation of transcription elongation. Guo M, Xu F, Yamada J, Egelhofer T, Gao Y, Hartzog GA, Teng M, Niu L. Structure 16, 1649-58, (2008). View articlePMID: 19000817
Representative structure
3lpe: Crystal structure of Spt4/5NGN heterodimer complex from Methanococcus jannaschii