NDLI: Reduction in DNA-binding affinity of Cys2His2 zinc finger proteins by linker phosphorylation

Content Provider	PubMed Central
Author	Jantz, Derek Berg, Jeremy M.
Copyright Year	2004
Abstract	Cys2His2 zinc finger proteins make up the largest class of transcription factors encoded in the genomes of higher eukaryotes. Recent studies of the Ikaros transcription factor demonstrated that this zinc finger protein undergoes cell cycle-dependent changes in association with DNA that seem to be due to phosphorylation of Thr or Ser residues in the linker regions connecting adjacent zinc finger domains. The high degree of conservation of this linker sequence within the Cys2His2 superfamily suggested a common mechanism for the cell cycle-dependent modulation of DNA-binding affinity throughout this large class of transcription factors. The effects of linker phosphorylation on DNA-binding affinity were investigated through a direct comparison of the DNA-binding properties of four synthetic zinc finger proteins produced by native chemical ligation. The four proteins, comprising three zinc finger domains joined by two consensus Thr-Gly-Glu-Lys-Pro linkers, correspond to all four possible combinations of linker Thr phosphorylation states. Fluorescence-based DNA-binding studies of a specific DNA-binding site revealed that phosphorylation of a single linker reduced binding affinity ≈40-fold, whereas phosphorylation of both linkers reduced binding affinity 130-fold. These results with purified components demonstrate that linker phosphorylation does, indeed, produce a significant reduction in DNA-binding affinity and support a model wherein a single cell cycle-dependent Ser/Thr kinase could simultaneously inactivate a large number of zinc finger transcription factors.
Related Links	http://dx.doi.org/10.1073/pnas.0402191101
Ending Page	7593
Page Count	5
Starting Page	7589
File Format	PDF
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	20
Volume Number	101
Language	English
Publisher	National Academy of Sciences
Publisher Date	2004-05-18
Access Restriction	Open
Rights Holder	National Academy of Sciences
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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

Reduction in DNA-binding affinity of Cys2His2 zinc finger proteins by linker phosphorylation.

De novo prediction of DNA-binding specificities for Cys2His2 zinc finger proteins

The prokaryotic Cys2His2 zinc-finger adopts a novel fold as revealed by the NMR structure of Agrobacterium tumefaciens Ros DNA-binding domain

A systematic survey of the Cys2His2 zinc finger DNA-binding landscape

Metal binding and folding properties of a minimalist Cys2His2 zinc finger peptide.

Balancing between affinity and speed in target DNA search by zinc-finger proteins via modulation of dynamic conformational ensemble

A systematic survey of the Cys2His2 zinc finger DNA-binding landscape

Probing the DNA-Binding Affinity and Specificity of Designed Zinc Finger Proteins

Highly efficient endonucleolytic cleavage of RNA by a Cys2His2 zinc-finger peptide

Reduction in DNA-binding affinity of Cys2His2 zinc finger proteins by linker phosphorylation

Similar Documents

Reduction in DNA-binding affinity of Cys2His2 zinc finger proteins by linker phosphorylation.

De novo prediction of DNA-binding specificities for Cys2His2 zinc finger proteins

The prokaryotic Cys2His2 zinc-finger adopts a novel fold as revealed by the NMR structure of Agrobacterium tumefaciens Ros DNA-binding domain

A systematic survey of the Cys2His2 zinc finger DNA-binding landscape

Metal binding and folding properties of a minimalist Cys2His2 zinc finger peptide.

Balancing between affinity and speed in target DNA search by zinc-finger proteins via modulation of dynamic conformational ensemble

A systematic survey of the Cys2His2 zinc finger DNA-binding landscape

Probing the DNA-Binding Affinity and Specificity of Designed Zinc Finger Proteins

Highly efficient endonucleolytic cleavage of RNA by a Cys2His2 zinc-finger peptide

Reduction in DNA-binding affinity of Cys2His2 zinc finger proteins by linker phosphorylation