Cysteine oxidation and disulfide formation in the ribosomal exit tunnel
Sign Up to like & getrecommendations! Published in 2020 at "Nature Communications"
DOI: 10.1038/s41467-020-19372-x
Abstract: Understanding the conformational sampling of translation-arrested ribosome nascent chain complexes is key to understand co-translational folding. Up to now, coupling of cysteine oxidation, disulfide bond formation and structure formation in nascent chains has remained elusive.… read more here.
Keywords: oxidation disulfide; exit tunnel; cysteine oxidation; formation ... See more keywords
An intrinsically disordered nascent protein interacts with specific regions of the ribosomal surface near the exit tunnel
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DOI: 10.1038/s42003-021-02752-4
Abstract: The influence of the ribosome on nascent chains is poorly understood, especially in the case of proteins devoid of signal or arrest sequences. Here, we provide explicit evidence for the interaction of specific ribosomal proteins… read more here.
Keywords: protein; exit tunnel; nascent protein; intrinsically disordered ... See more keywords
Critical 23S rRNA interactions for macrolide-dependent ribosome stalling on the ErmCL nascent peptide chain
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DOI: 10.1093/nar/gkx195
Abstract: Abstract The nascent peptide exit tunnel has recently been identified as a functional region of ribosomes contributing to translation regulation and co-translational protein folding. Inducible expression of the erm resistance genes depends on ribosome stalling… read more here.
Keywords: ribosome stalling; exit tunnel; peptide; nascent peptide ... See more keywords
The force-sensing peptide VemP employs extreme compaction and secondary structure formation to induce ribosomal stalling
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DOI: 10.7554/elife.25642
Abstract: Interaction between the nascent polypeptide chain and the ribosomal exit tunnel can modulate the rate of translation and induce translational arrest to regulate expression of downstream genes. The ribosomal tunnel also provides a protected environment… read more here.
Keywords: exit tunnel; secondary structure; formation; structure ... See more keywords