RNA sequence- and shape-dependent recognition by proteins in the ribonucleoprotein particle

ŠTEFL, Richard; Lenka SKŘÍŠOVSKÁ and Frederic ALLAIN. RNA sequence- and shape-dependent recognition by proteins in the ribonucleoprotein particle. EMBO REPORTS. 2005, vol. 6, No 1, p. 33-38. ISSN 1469-221X.

Basic information

Original name

RNA sequence- and shape-dependent recognition by proteins in the ribonucleoprotein particle

Name in Czech

RNA sequence- and shape-dependent recognition by proteins in the ribonucleoprotein particle

Authors

ŠTEFL, Richard; Lenka SKŘÍŠOVSKÁ and Frederic ALLAIN

Edition

EMBO REPORTS, 2005, 1469-221X

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Other information

Language

English

Type of outcome

Article in a journal

Field of Study

10600 1.6 Biological sciences

Country of publisher

United Kingdom of Great Britain and Northern Ireland

Confidentiality degree

is not subject to a state or trade secret

Impact factor

Impact factor: 7.663

Organization unit

Faculty of Science

UT WoS

000226183500009

Keywords in English

DOUBLE-STRANDED-RNA; ZINC-FINGER PROTEIN; PRE-RIBOSOMAL-RNA; HUMAN U1A PROTEIN; AU-RICH ELEMENT; BINDING DOMAIN; CRYSTAL-STRUCTURE; STRUCTURAL BASIS; DNA RECOGNITION;

Tags

AU-RICH ELEMENT, BINDING DOMAIN, CRYSTAL-STRUCTURE, DNA RECOGNITION, DOUBLE-STRANDED-RNA, HUMAN U1A PROTEIN, PRE-RIBOSOMAL-RNA, STRUCTURAL BASIS, ZINC-FINGER PROTEIN

Tags

International impact, Reviewed

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Abstract

In the original language

At all stages of its life ( from transcription to translation), an RNA transcript interacts with many different RNA-binding proteins. The composition of this supramolecular assembly, known as a ribonucleoprotein particle, is diverse and highly dynamic. RNA-binding proteins control the generation, maturation and lifespan of the RNA transcript and thus regulate and influence the cellular function of the encoded gene. Here, we review our current understanding of protein-RNA recognition mediated by the two most abundant RNA-binding domains (the RNA-recognition motif and the double-stranded RNA-binding motif) plus the zinc-finger motif, the most abundant nucleic-acid-binding domain. In addition, we discuss how not only the sequence but also the shape of the RNA are recognized by these three classes of RNA-binding protein.

In Czech

At all stages of its life ( from transcription to translation), an RNA transcript interacts with many different RNA-binding proteins. The composition of this supramolecular assembly, known as a ribonucleoprotein particle, is diverse and highly dynamic. RNA-binding proteins control the generation, maturation and lifespan of the RNA transcript and thus regulate and influence the cellular function of the encoded gene. Here, we review our current understanding of protein-RNA recognition mediated by the two most abundant RNA-binding domains (the RNA-recognition motif and the double-stranded RNA-binding motif) plus the zinc-finger motif, the most abundant nucleic-acid-binding domain. In addition, we discuss how not only the sequence but also the shape of the RNA are recognized by these three classes of RNA-binding protein.