Literature DB >> 1689291

Assembly and disassembly of the Drosophila RNA polymerase II complex during transcription.

J T Kadonaga1.   

Abstract

Initiation of mRNA synthesis by RNA polymerase II occurs by a multistep pathway that involves the polymerase along with several auxiliary factors. Here I describe an analysis of the kinetics and mechanism of action of Drosophila RNA polymerase II by using the detergent Sarkosyl to inhibit different steps in the pathway leading to transcription initiation. The template DNA and Drosophila transcription factors assemble into a partially Sarkosyl-resistant initiation complex with a kinetically first order time course characterized by a t1/2 of about 3 min, and subsequent conversion of the initiation complex into the elongating complex occurs rapidly (less than 5 s). During the formation of the first two phosphodiester bonds, there is a stepwise transition from the initiation complex to the 0.25% Sarkosyl-resistant elongating polymerase. In contrast to the mammalian RNA polymerase II systems, the Drosophila extracts possess the ability to carry out many rounds (approximately 10) of transcription in vitro. Finally, the transcription factors are committed to the template DNA as an initiation complex, but then no longer appear to remain committed to the DNA after initiation of transcription. This finding suggests that there is complete assembly and disassembly of the transcription complex during each round of transcription by RNA polymerase II.

Entities:  

Mesh:

Substances:

Year:  1990        PMID: 1689291

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  48 in total

1.  Fast kinetics of chromatin assembly revealed by single-molecule videomicroscopy and scanning force microscopy.

Authors:  B Ladoux; J P Quivy; P Doyle; O du Roure; G Almouzni; J L Viovy
Journal:  Proc Natl Acad Sci U S A       Date:  2000-12-19       Impact factor: 11.205

2.  Periodic binding of individual core histones to DNA: inadvertent purification of the core histone H2B as a putative enhancer-binding factor.

Authors:  L A Kerrigan; J T Kadonaga
Journal:  Nucleic Acids Res       Date:  1992-12-25       Impact factor: 16.971

3.  Mechanism by which the IFN-beta enhanceosome activates transcription.

Authors:  J Yie; K Senger; D Thanos
Journal:  Proc Natl Acad Sci U S A       Date:  1999-11-09       Impact factor: 11.205

4.  Control of formation of two distinct classes of RNA polymerase II elongation complexes.

Authors:  N F Marshall; D H Price
Journal:  Mol Cell Biol       Date:  1992-05       Impact factor: 4.272

5.  Cell-free system for assembly of transcriptionally repressed chromatin from Drosophila embryos.

Authors:  P B Becker; C Wu
Journal:  Mol Cell Biol       Date:  1992-05       Impact factor: 4.272

6.  RNA polymerase II elongation complex. Elongation complexes purified using an anti-RNA antibody do not contain initiation factor alpha.

Authors:  D Reines
Journal:  J Biol Chem       Date:  1991-06-05       Impact factor: 5.157

7.  Drosophila P-element transposase is a transcriptional repressor in vitro.

Authors:  P D Kaufman; D C Rio
Journal:  Proc Natl Acad Sci U S A       Date:  1991-04-01       Impact factor: 11.205

8.  The double bromodomain proteins Brd2 and Brd3 couple histone acetylation to transcription.

Authors:  Gary LeRoy; Brenden Rickards; S J Flint
Journal:  Mol Cell       Date:  2008-04-11       Impact factor: 17.970

9.  Regulation of the p53 transcriptional response by structurally diverse core promoters.

Authors:  José M Morachis; Christopher M Murawsky; Beverly M Emerson
Journal:  Genes Dev       Date:  2009-12-29       Impact factor: 11.361

10.  Sequence of ornithine decarboxylase from Lactobacillus sp. strain 30a.

Authors:  M L Hackert; D W Carroll; L Davidson; S O Kim; C Momany; G L Vaaler; L Zhang
Journal:  J Bacteriol       Date:  1994-12       Impact factor: 3.490

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.