NDLI: The Functions of TFIIF during Initiation and Transcript Elongation Are Differentially Affected by Phosphorylation by Casein Kinase 2*

Content Provider	PubMed Central
Author	Újvári, Andrea Pal, Mahadeb Luse, Donal S.
Copyright Year	2011
Abstract	The RNA polymerase II (pol II) initiation and elongation factor elongation factor TFIIF can be extensively phosphorylated in vivo, although the significance of this modification has not been clear. We now show that phosphorylation of recombinant TFIIF by casein kinase 2 (CK2) reduces or eliminates some of the functions of TFIIF while paradoxically leaving others intact. Phospho-IIF is fully functional in binding to free pol II and is able to support the initiation of transcription. However, the phosphorylated factor does not bind to stalled elongation complexes as measured in a gel mobility shift assay. Significantly, phosphorylation strongly reduces (or for some truncated versions of RAP74, eliminates) stimulation of transcript elongation by TFIIF. Thus, although TFIIF must participate at the initiation of transcription, its ability to continue its association with pol II and stimulate transcript elongation can be specifically regulated by CK2. This is particularly interesting because CK2 is required for initiation at a subset of pol II promoters. Modulation of TFIIF function could be important in controlling promoter-proximal pausing by pol II during the early stage of transcript elongation.
Related Links	http://dx.doi.org/10.1074/jbc.m110.205658
Ending Page	23167
Page Count	8
Starting Page	23160
File Format	PDF
ISSN	00219258
e-ISSN	1083351X
Journal	The Journal of Biological Chemistry
Issue Number	26
Volume Number	286
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	2011-07-01
Access Restriction	Open
Rights Holder	American Society for Biochemistry and Molecular Biology
Subject Keyword	Cell Biology Biochemistry Molecular Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

The Functions of TFIIF during Initiation and Transcript Elongation Are Differentially Affected by Phosphorylation by Casein Kinase 2

Phosphorylation of Maize Eukaryotic Translation Initiation Factor 5A (eIF5A) by Casein Kinase 2

Phosphorylation of fibrinogen by casein kinase 2.

Phosphorylation of elongation factor-2 kinase differentially regulates the enzyme’s stability under stress conditions

Regulation of casein kinase 2 by phosphorylation/dephosphorylation.

Phosphorylation of elf-2(3 and ef-1 by two ribosoflial kinase fractions

Phosphorylation of elf-2(3 and ef-1 by two ribosoflial kinase fractions

Phosphorylation of elf-2(3 and ef-1 by two ribosoflial kinase fractions

Casein Kinase 2 Phosphorylation of Protein Kinase C and Casein Kinase 2 Substrate in Neurons (PACSIN) 1 Protein Regulates Neuronal Spine Formation*

The Functions of TFIIF during Initiation and Transcript Elongation Are Differentially Affected by Phosphorylation by Casein Kinase 2*

Similar Documents

The Functions of TFIIF during Initiation and Transcript Elongation Are Differentially Affected by Phosphorylation by Casein Kinase 2

Phosphorylation of Maize Eukaryotic Translation Initiation Factor 5A (eIF5A) by Casein Kinase 2

Phosphorylation of fibrinogen by casein kinase 2.

Phosphorylation of elongation factor-2 kinase differentially regulates the enzyme’s stability under stress conditions

Regulation of casein kinase 2 by phosphorylation/dephosphorylation.

Phosphorylation of elf-2(3 and ef-1 by two ribosoflial kinase fractions

Phosphorylation of elf-2(3 and ef-1 by two ribosoflial kinase fractions

Phosphorylation of elf-2(3 and ef-1 by two ribosoflial kinase fractions

Casein Kinase 2 Phosphorylation of Protein Kinase C and Casein Kinase 2 Substrate in Neurons (PACSIN) 1 Protein Regulates Neuronal Spine Formation*

The Functions of TFIIF during Initiation and Transcript Elongation Are Differentially Affected by Phosphorylation by Casein Kinase 2*