Viewing folding of nascent polypeptide chains from ribosomes
نویسندگان
چکیده
منابع مشابه
Viewing folding of nascent polypeptide chains from ribosomes.
Regulation of gene expression occurs at multiple stages and ultimately determines the protein levels in cells. The last decade has witnessed impressive progress in the development of approaches to measuring changes in cellular transcription and protein complement. However, techniques monitoring protein synthesis have lagged far behind. Current proteomic studies gauge the steady state levels of ...
متن کاملStructure and folding of nascent polypeptide chains during protein translocation in the endoplasmic reticulum.
To investigate the role of protein folding and chaperone-nascent chain interactions in translocation across the endoplasmic reticulum membrane, the translocation of wild type and mutant forms of preprolactin were studied in vivo and in vitro. The preprolactin mutant studied contains an 18-amino acid substitution at the amino terminus of the mature protein, eliminating a disulfide-bonded loop do...
متن کاملNascent Ribosomes
The conversion of a ribosomal RNA transcript to a cytoplasmic ribosome requires hundreds of accessory RNA and protein factors. Two papers published recently in Molecular Cell provide first looks at the association of these processing factors with the intermediates in ribosome synthesis (Harnpicharnchai et al., 2001; Bassler et al., 2001).
متن کاملBirth, life and death of nascent polypeptide chains
The journey of nascent polypeptides from synthesis at the peptidyl transferase center of the ribosome ("birth") to full function ("maturity") involves multiple interactions, constraints, modifications and folding events. Each step of this journey impacts the ultimate expression level and functional capacity of the translated protein. It has become clear that the kinetics of protein translation ...
متن کاملMechanism of puromycin action: fate of ribosomes after release of nascent protein chains from polysomes.
The exchange of ribosomal subunits during the release of growing polypeptide chains by puromycin has been investigated in a bacterial cell-free system engaged in protein synthesis. The addition of spermidine, used as a stabilizing agent of 70S monomers, caused a strong inhibition of the subunit exchange. This result led us to conclude that upon premature release of unfinished protein chains by ...
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: Expert Review of Proteomics
سال: 2012
ISSN: 1478-9450,1744-8387
DOI: 10.1586/epr.12.57