Literature DB >> 15853796

The double-stranded RNA-binding motif, a versatile macromolecular docking platform.

Kung-Yao Chang1, Andres Ramos.   

Abstract

The double-stranded RNA-binding motif (dsRBM) is an alphabetabetabetaalpha fold with a well-characterized function to bind structured RNA molecules. This motif is widely distributed in eukaryotic proteins, as well as in proteins from bacteria and viruses. dsRBM-containing proteins are involved in processes ranging from RNA editing to protein phosphorylation in translational control and contain a variable number of dsRBM domains. The structural work of the past five years has identified a common mode of RNA target recognition by dsRBMs and dissected this recognition into two functionally separated interaction modes. The first involves the recognition of specific moieties of the RNA A-form helix by two protein loops, while the second is based on the interaction between structural elements flanking the RNA duplex with the first helix of the dsRBM. The latter interaction can be tuned by other protein elements. Recent work has made clear that dsRBMs can also recognize non-RNA targets (proteins and DNA), and act in combination with other dsRBMs and non-dsRBM motifs to play a regulatory role in catalytic processes. The elucidation of functional networks coordinated by dsRBM folds will require information on the precise functional relationship between different dsRBMs and a clarification of the principles underlying dsRBM-protein recognition.

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Year:  2005        PMID: 15853796     DOI: 10.1111/j.1742-4658.2005.04652.x

Source DB:  PubMed          Journal:  FEBS J        ISSN: 1742-464X            Impact factor:   5.542


  66 in total

Review 1.  Deciphering the role of RNA-binding proteins in the post-transcriptional control of gene expression.

Authors:  Shivendra Kishore; Sandra Luber; Mihaela Zavolan
Journal:  Brief Funct Genomics       Date:  2010-12-01       Impact factor: 4.241

2.  Minor-groove-modulating adenosine replacements control protein binding and RNAi activity in siRNAs.

Authors:  Hayden Peacock; Erik Fostvedt; Peter A Beal
Journal:  ACS Chem Biol       Date:  2010-10-07       Impact factor: 5.100

3.  High affinity, dsRNA binding by disconnected interacting protein 1.

Authors:  Daniel J Catanese; Kathleen S Matthews
Journal:  Biochem Biophys Res Commun       Date:  2010-07-17       Impact factor: 3.575

4.  Dynamic origins of differential RNA binding function in two dsRBDs from the miRNA "microprocessor" complex.

Authors:  Christopher Wostenberg; Kaycee A Quarles; Scott A Showalter
Journal:  Biochemistry       Date:  2010-11-22       Impact factor: 3.162

5.  Dimerization of ADAR2 is mediated by the double-stranded RNA binding domain.

Authors:  Hanne Poulsen; Rasmus Jorgensen; Anders Heding; Finn C Nielsen; Bjarne Bonven; Jan Egebjerg
Journal:  RNA       Date:  2006-05-08       Impact factor: 4.942

6.  The dsRNA binding site of human Toll-like receptor 3.

Authors:  Jessica K Bell; Janine Askins; Pamela R Hall; David R Davies; David M Segal
Journal:  Proc Natl Acad Sci U S A       Date:  2006-05-23       Impact factor: 11.205

Review 7.  RNA-binding proteins: modular design for efficient function.

Authors:  Bradley M Lunde; Claire Moore; Gabriele Varani
Journal:  Nat Rev Mol Cell Biol       Date:  2007-06       Impact factor: 94.444

8.  An extra double-stranded RNA binding domain confers high activity to a squid RNA editing enzyme.

Authors:  Juan Pablo Palavicini; Mary A O'Connell; Joshua J C Rosenthal
Journal:  RNA       Date:  2009-04-23       Impact factor: 4.942

9.  The double-stranded RNA binding domain of the vaccinia virus E3L protein inhibits both RNA- and DNA-induced activation of interferon beta.

Authors:  Jean-Baptiste Marq; Stéphane Hausmann; Jeremy Luban; Daniel Kolakofsky; Dominique Garcin
Journal:  J Biol Chem       Date:  2009-07-07       Impact factor: 5.157

10.  The RNA silencing endonuclease Argonaute 2 mediates specific antiviral immunity in Drosophila melanogaster.

Authors:  Ronald P van Rij; Maria-Carla Saleh; Bassam Berry; Catherine Foo; Andrew Houk; Christophe Antoniewski; Raul Andino
Journal:  Genes Dev       Date:  2006-11-01       Impact factor: 11.361

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