Solution structure of conserved AGNN tetraloops: insights into Rnt1p RNA processing
نویسندگان
چکیده
منابع مشابه
A new alpha-helical extension promotes RNA binding by the dsRBD of Rnt1p RNAse III.
Rnt1 endoribonuclease, the yeast homolog of RNAse III, plays an important role in the maturation of a diverse set of RNAs. The enzymatic activity requires a conserved catalytic domain, while RNA binding requires the double-stranded RNA-binding domain (dsRBD) at the C-terminus of the protein. While bacterial RNAse III enzymes cleave double-stranded RNA, Rnt1p specifically cleaves RNAs that posse...
متن کاملStructural basis for recognition of the AGNN tetraloop RNA fold by the double-stranded RNA-binding domain of Rnt1p RNase III.
Specific recognition of double-stranded RNA (dsRNA) by dsRNA-binding domains (dsRBDs) is involved in a large number of biological and regulatory processes. Although structures of dsRBDs in complex with dsRNA have revealed how they can bind to dsRNA in general, these do not explain how a dsRBD can recognize specific RNAs. Rnt1p, a member of the RNase III family of dsRNA endonucleases, is a key c...
متن کاملRecognition of a conserved class of RNA tetraloops by Saccharomyces cerevisiae RNase III.
Ribonucleases III are double-stranded RNA (dsRNA) endonucleases required for the processing of a large number of prokaryotic and eukaryotic transcripts. Although the specificity of bacterial RNase III cleavage relies on antideterminants in the dsRNA, the molecular basis of eukaryotic RNase III specificity is unknown. All substrates of yeast RNase III (Rnt1p) are capped by terminal tetraloops sh...
متن کاملStructure of a yeast RNase III dsRBD complex with a noncanonical RNA substrate provides new insights into binding specificity of dsRBDs.
dsRBDs often bind dsRNAs with some specificity, yet the basis for this is poorly understood. Rnt1p, the major RNase III in Saccharomyces cerevisiae, cleaves RNA substrates containing hairpins capped by A/uGNN tetraloops, using its dsRBD to recognize a conserved tetraloop fold. However, the identification of a Rnt1p substrate with an AAGU tetraloop raised the question of whether Rnt1p binds to t...
متن کاملConservation of RNase III processing pathways and specificity in hemiascomycetes.
Rnt1p, the only known Saccharomyces cerevisiae RNase III endonuclease, plays important functions in the processing of precursors of rRNAs (pre-rRNAs) and of a large number of small nuclear RNAs (snRNAs) and small nucleolar RNAs (snoRNAs). While most eukaryotic RNases III, including the Schizosaccharomyces pombe enzyme Pac1p, cleave double-stranded RNA without sequence specificity, Rnt1p cleavag...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: The EMBO Journal
سال: 2001
ISSN: 1460-2075
DOI: 10.1093/emboj/20.24.7250