Internal loop mutations in the ribosomal protein L30 binding site of the yeast L30 RNA transcript
نویسندگان
چکیده
منابع مشابه
Internal loop mutations in the ribosomal protein L30 binding site of the yeast L30 RNA transcript.
Yeast ribosomal protein L30 binds to an asymmetric, purine-rich internal loop in its transcript to repress its own splicing and translation. The protein-bound form of the stem-internal loop-stem RNA is an example of a kink-turn RNA structural motif. Analysis of kink-turn motifs reveals that in (2 + 5) internal loops, the identities of five nucleotides are very important, while the remaining two...
متن کاملAssignment of the L30-mRNA complex using selective isotopic labeling and RNA mutants.
The helix-loop-helix structure formed in the pre-mRNA and the mRNA of L30, a ribosomal protein from the yeast Saccharomyces cerevisiae, serves as an auto-regulatory binding site for the protein to suppress the L30 synthesis upon overproduction. Using a 33-nucleotide model RNA, the structures of the L30 binding site RNA in the presence and absence of the protein were investigated using nuclear m...
متن کاملCharacterization of the pre-mRNA binding site for yeast ribosomal protein L32: the importance of a purine-rich internal loop.
The structure of the RNA binding target for Saccharomyces cerevisiae ribosomal protein L32 was examined using chemical and enzymatic probes as well as thermodynamic methods. In vivo, the production of yeast RPL32 is regulated by a feedback mechanism whereby RPL32 binds to the 5' end of its transcript and inhibits splicing. The binding site of ribosomal protein L32 on the L32 RNA transcript can ...
متن کاملInherent protein structural flexibility at the RNA-binding interface of L30e.
The Saccharomyces cerevisiae ribosomal protein L30 autoregulates its own expression by binding to a purine-rich internal loop in its pre-mRNA and mRNA. NMR studies of L30 and its RNA complex showed that both the internal loop of the RNA as well as a region of the protein become substantially more ordered upon binding. A crystal structure of a maltose binding protein (MBP)-L30 fusion protein wit...
متن کاملL30 binds the nascent RPL30 transcript to repress U2 snRNP recruitment.
The mechanisms of pre-mRNA splicing regulation are poorly understood. Here we dissect how the Saccharomyces cerevisiae ribosomal L30 protein blocks splicing of its pre-mRNA upon binding a kink-turn structure including the 5' splice site. We show that L30 binds the nascent RPL30 transcript without preventing recognition of the 5' splice site by U1 snRNP but blocking U2 snRNP association with the...
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ژورنال
عنوان ژورنال: RNA
سال: 2004
ISSN: 1355-8382
DOI: 10.1261/rna.2159504