Literature DB >> 11024112

Structural phosphoprotein M2-1 of the human respiratory syncytial virus is an RNA binding protein.

I Cuesta1, X Geng, A Asenjo, N Villanueva.   

Abstract

The structural phosphoprotein M2-1 of human respiratory syncytial virus (HRSV) Long strain shows RNA binding capacity in three different assays that detect RNA-protein complexes: cross-linking, gel retardation, and Northern-Western assays. It is able to bind HRSV leader RNA specifically with cooperative kinetics, with an apparent K(d) of at least 90 nM. It also binds to long RNAs with no sequence specificity. The RNA binding domain has been located between amino acid residues 59 and 85, at the NH(2) terminus of the protein. This region contains the phosphorylatable amino acid residues threonine 56 and serine 58, whose modification decreases the binding capacity of M2-1 protein to long RNAs.

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Year:  2000        PMID: 11024112      PMCID: PMC102022          DOI: 10.1128/jvi.74.21.9858-9867.2000

Source DB:  PubMed          Journal:  J Virol        ISSN: 0022-538X            Impact factor:   5.103


  38 in total

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Authors:  J S Park; M Wang; S J Park; S H Lee
Journal:  J Biol Chem       Date:  1999-10-08       Impact factor: 5.157

5.  Effects of intercistronic length on the efficiency of reinitiation by eucaryotic ribosomes.

Authors:  M Kozak
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6.  Prediction of protein conformation.

Authors:  P Y Chou; G D Fasman
Journal:  Biochemistry       Date:  1974-01-15       Impact factor: 3.162

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Journal:  Virus Res       Date:  1985-03       Impact factor: 3.303

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Authors:  R W Hardy; G W Wertz
Journal:  J Virol       Date:  2000-07       Impact factor: 5.103

10.  Protein-blotting on Polybrene-coated glass-fiber sheets. A basis for acid hydrolysis and gas-phase sequencing of picomole quantities of protein previously separated on sodium dodecyl sulfate/polyacrylamide gel.

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  24 in total

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Journal:  J Virol       Date:  2006-07       Impact factor: 5.103

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Journal:  J Virol       Date:  2014-04-23       Impact factor: 5.103

3.  Respiratory syncytial virus M2-1 protein requires phosphorylation for efficient function and binds viral RNA during infection.

Authors:  T L Cartee; G W Wertz
Journal:  J Virol       Date:  2001-12       Impact factor: 5.103

4.  Crystal structure of the essential transcription antiterminator M2-1 protein of human respiratory syncytial virus and implications of its phosphorylation.

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Journal:  Proc Natl Acad Sci U S A       Date:  2014-01-13       Impact factor: 11.205

5.  Zinc binding activity of human metapneumovirus M2-1 protein is indispensable for viral replication and pathogenesis in vivo.

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Journal:  J Virol       Date:  2015-04-08       Impact factor: 5.103

6.  Requirement of cysteines and length of the human respiratory syncytial virus M2-1 protein for protein function and virus viability.

Authors:  R S Tang; N Nguyen; X Cheng; H Jin
Journal:  J Virol       Date:  2001-12       Impact factor: 5.103

7.  Interaction between human respiratory syncytial virus (RSV) M2-1 and P proteins is required for reconstitution of M2-1-dependent RSV minigenome activity.

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Journal:  J Virol       Date:  2003-10       Impact factor: 5.103

8.  Identification of RNA-binding regions on the P and V proteins of human parainfluenza virus type 2.

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9.  Biophysical and Dynamic Characterization of Fine-Tuned Binding of the Human Respiratory Syncytial Virus M2-1 Core Domain to Long RNAs.

Authors:  Icaro P Caruso; Giovana C Guimarães; Vitor B Machado; Marcelo A Fossey; Dieter Willbold; Fabio C L Almeida; Fátima P Souza
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10.  The respiratory syncytial virus M2-1 protein forms tetramers and interacts with RNA and P in a competitive manner.

Authors:  Thi-Lan Tran; Nathalie Castagné; Virginie Dubosclard; Sylvie Noinville; Emmanuelle Koch; Mohammed Moudjou; Céline Henry; Julie Bernard; Robert Paul Yeo; Jean-François Eléouët
Journal:  J Virol       Date:  2009-04-22       Impact factor: 5.103

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