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

ŠTEFL, Richard, Lenka SKŘÍŠOVSKÁ a Frederic ALLAIN. RNA sequence- and shape-dependent recognition by proteins in the ribonucleoprotein particle. EMBO REPORTS. 2005, roč. 6, č. 1, s. 33-38. ISSN 1469-221X.

Základní údaje

• Originální název: RNA sequence- and shape-dependent recognition by proteins in the ribonucleoprotein particle
• Název česky: RNA sequence- and shape-dependent recognition by proteins in the ribonucleoprotein particle
• Autoři: ŠTEFL, Richard, Lenka SKŘÍŠOVSKÁ a Frederic ALLAIN.
• Vydání: EMBO REPORTS, 2005, 1469-221X.

Další údaje

• Originální jazyk: angličtina
• Typ výsledku: Článek v odborném periodiku
• Obor: 10600 1.6 Biological sciences
• Stát vydavatele: Velká Británie a Severní Irsko
• Utajení: není předmětem státního či obchodního tajemství
• Impakt faktor: Impact factor: 7.663
• Organizační jednotka: Přírodovědecká fakulta
• UT WoS: 000226183500009
• Klíčová slova anglicky: DOUBLE-STRANDED-RNA; ZINC-FINGER PROTEIN; PRE-RIBOSOMAL-RNA; HUMAN U1A PROTEIN; AU-RICH ELEMENT; BINDING DOMAIN; CRYSTAL-STRUCTURE; STRUCTURAL BASIS; DNA RECOGNITION
• Štítky: AU-RICH ELEMENT, BINDING DOMAIN, CRYSTAL-STRUCTURE, DNA RECOGNITION, DOUBLE-STRANDED-RNA, HUMAN U1A PROTEIN, PRE-RIBOSOMAL-RNA, STRUCTURAL BASIS, ZINC-FINGER PROTEIN
• Příznaky: Mezinárodní význam, Recenzováno

Anotace

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.

Anotace česky

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.