NDLI: RNA recognition and self-association of CPEB4 is mediated by its tandem RRM domains

Content Provider	PubMed Central
Author	Schelhorn, Constanze Gordon, James M. B. Ruiz, Lidia Alguacil, Javier Pedroso, Enrique Macias, Maria J.
Copyright Year	2014
Abstract	Cytoplasmic polyadenylation is regulated by the interaction of the cytoplasmic polyadenylation element binding proteins (CPEB) with cytoplasmic polyadenylation element (CPE) containing mRNAs. The CPEB family comprises four paralogs, CPEB1–4, each composed of a variable N-terminal region, two RNA recognition motif (RRM) and a C-terminal ZZ-domain. We have characterized the RRM domains of CPEB4 and their binding properties using a combination of biochemical, biophysical and NMR techniques. Isothermal titration calorimetry, NMR and electrophoretic mobility shift assay experiments demonstrate that both the RRM domains are required for an optimal CPE interaction and the presence of either one or two adenosines in the two most commonly used consensus CPE motifs has little effect on the affinity of the interaction. Both the single RRM1 and the tandem RRM1–RRM2 have the ability to dimerize, although representing a minor population. Self-association does not affect the proteins’ ability to interact with RNA as demonstrated by ion mobility–mass spectrometry. Chemical shift effects measured by NMR of the apo forms of the RRM1–RRM2 samples indicate that the two domains are orientated toward each other. NMR titration experiments show that residues on the β-sheet surface on RRM1 and at the C-terminus of RRM2 are affected upon RNA binding. We propose a model of the CPEB4 RRM1–RRM2–CPE complex that illustrates the experimental data.
Related Links	http://dx.doi.org/10.1093/nar/gku700
Ending Page	10195
Page Count	11
Starting Page	10185
File Format	PDF
ISSN	13624962
e-ISSN	13624962
Journal	Nucleic Acids Research
Issue Number	15
Volume Number	42
Language	English
Publisher	Oxford University Press
Publisher Date	2014-09-02
Access Restriction	Open
Rights Holder	Oxford University Press
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Genetics

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

RNA recognition and self-association of CPEB4 is mediated by its tandem RRM domains

Structural basis for RNA recognition by the N-terminal tandem RRM domains of human RBM45

Thermodynamic Coupling of the tandem RRM domains of hnRNP A1 underlie its Pleiotropic RNA Binding Functions

Self-association of the erythroid transcription factor GATA-1 mediated by its zinc finger domains.

Recognition of viral RNA stem–loops by the tandem double-stranded RNA binding domains of PKR

The binding of TIA-1 to RNA C-rich sequences is driven by its C-terminal RRM domain

ZBP1 subcellular localization and association with stress granules is controlled by its Z-DNA binding domains

Structural basis for the dual RNA-recognition modes of human Tra2-β RRM

Structural Dynamics of the GW182 Silencing Domain Including its RNA Recognition motif (RRM) Revealed by Hydrogen-Deuterium Exchange Mass Spectrometry

RNA recognition and self-association of CPEB4 is mediated by its tandem RRM domains

Similar Documents

RNA recognition and self-association of CPEB4 is mediated by its tandem RRM domains

Structural basis for RNA recognition by the N-terminal tandem RRM domains of human RBM45

Thermodynamic Coupling of the tandem RRM domains of hnRNP A1 underlie its Pleiotropic RNA Binding Functions

Self-association of the erythroid transcription factor GATA-1 mediated by its zinc finger domains.

Recognition of viral RNA stem–loops by the tandem double-stranded RNA binding domains of PKR

The binding of TIA-1 to RNA C-rich sequences is driven by its C-terminal RRM domain

ZBP1 subcellular localization and association with stress granules is controlled by its Z-DNA binding domains

Structural basis for the dual RNA-recognition modes of human Tra2-β RRM

Structural Dynamics of the GW182 Silencing Domain Including its RNA Recognition motif (RRM) Revealed by Hydrogen-Deuterium Exchange Mass Spectrometry

RNA recognition and self-association of CPEB4 is mediated by its tandem RRM domains