Elongation by RNA polymerase II: the short and long of it

被引:544
作者
Sim, RJ
Belotserkovskaya, R
Reinberg, D [1 ]
机构
[1] Univ Med & Dent New Jersey, Robert Wood Johnson Med Sch, Howard Hughes Med Inst, Piscataway, NJ 08854 USA
[2] Univ Med & Dent New Jersey, Robert Wood Johnson Med Sch, Dept Biochem, Div Nucle Acids Enzymol, Piscataway, NJ 08854 USA
关键词
elongation; transcription; RNA polymerase II; chromatin CTD;
D O I
10.1101/gad.1235904
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Appreciable advances into the process of transcript elongation by RNA polymerase II (RNAP II) have identified this stage as a dynamic and highly regulated step of the transcription cycle. Here, we discuss the many factors that regulate the elongation stage of transcription. Our discussion includes the classical elongation factors that modulate the activity of RNAP II, and the more recently identified factors that facilitate elongation on chromatin templates. Additionally, we discuss the factors that associate with RNAP II, but do not modulate its catalytic activity. Elongation is highlighted as a central process that coordinates multiple stages in mRNA biogenesis and maturation.
引用
收藏
页码:2437 / 2468
页数:32
相关论文
共 367 条
[1]   Phosphorylation of serine 2 within the RNA polymerase IIC-terminal domain couples transcription and 3′ end processing [J].
Ahn, SH ;
Kim, M ;
Buratowski, S .
MOLECULAR CELL, 2004, 13 (01) :67-76
[2]   REQUIREMENT FOR TFIIH KINASE-ACTIVITY IN TRANSCRIPTION BY RNA-POLYMERASE-II [J].
AKOULITCHEV, S ;
MAKELA, TP ;
WEINBERG, RA ;
REINBERG, D .
NATURE, 1995, 377 (6549) :557-560
[3]   A role for chromatin remodeling in transcriptional termination by RNA polymerase II [J].
Alén, C ;
Kent, NA ;
Jones, HS ;
O'Sullivan, J ;
Aranda, A ;
Proudfoot, NJ .
MOLECULAR CELL, 2002, 10 (06) :1441-1452
[4]   High-resolution localization of Drosophila Spt5 and Spt6 at heat shock genes in vivo:: roles in promoter proximal pausing and transcription elongation [J].
Andrulis, ED ;
Guzmán, E ;
Döring, P ;
Werner, J ;
Lis, JT .
GENES & DEVELOPMENT, 2000, 14 (20) :2635-2649
[5]   The RNA processing exosome is linked to elongating RNA polymerase II in Drosophila [J].
Andrulis, ED ;
Werner, J ;
Nazarian, A ;
Erdjument-Bromage, H ;
Tempst, P ;
Lis, JT .
NATURE, 2002, 420 (6917) :837-841
[6]   FCP1, the RAP74-interacting subunit of a human protein phosphatase that dephosphorylates the carboxyl-terminal domain of RNA polymerase IIO [J].
Archambault, J ;
Pan, GH ;
Dahmus, GK ;
Cartier, M ;
Marshall, N ;
Zhang, S ;
Dahmus, ME ;
Greenblatt, J .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (42) :27593-27601
[7]   An essential component of a C-terminal domain phosphatase that interacts with transcription factor IIF in Saccharomyces cerevisiae [J].
Archambault, J ;
Chambers, RS ;
Kobor, MS ;
Ho, Y ;
Cartier, M ;
Bolotin, D ;
Andrews, B ;
Kane, CM ;
Greenblatt, J .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1997, 94 (26) :14300-14305
[8]   Architecture of initiation-competent 12-subunit RNA polymerase II [J].
Armache, KJ ;
Kettenberger, H ;
Cramer, P .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2003, 100 (12) :6964-6968
[9]   The Drosophila BRM complex facilitates global transcription by RNA polymerase II [J].
Armstrong, JA ;
Papoulas, O ;
Daubresse, G ;
Sperling, AS ;
Lis, JT ;
Scott, MP ;
Tamkun, JW .
EMBO JOURNAL, 2002, 21 (19) :5245-5254
[10]   The inducible elongin A elongation activation domain: Structure, function and interaction with the elongin BC complex [J].
Aso, T ;
Haque, D ;
Barstead, RJ ;
Conaway, RC ;
Conaway, JW .
EMBO JOURNAL, 1996, 15 (20) :5557-5566