Journal ArticleDOI
Role of a Peptide Tagging System in Degradation of Proteins Synthesized from Damaged Messenger RNA
TLDR
Variants of λ repressor and cytochrome b562 translated from messenger RNAs without stop codons were modified by carboxyl terminal addition of an ssrA-encoded peptide tag and subsequently degraded by car boxyl terminal-specific proteases present in both the cytoplasm and periplasm of Escherichia coli.Abstract:
Variants of lambda repressor and cytochrome b562 translated from messenger RNAs without stop codons were modified by carboxyl terminal addition of an ssrA-encoded peptide tag and subsequently degraded by carboxyl terminal-specific proteases present in both the cytoplasm and periplasm of Escherichia coli. The tag appears to be added to the carboxyl terminus of the nascent polypeptide chain by cotranslational switching of the ribosome from the damaged messenger RNA to ssrA RNA.read more
Citations
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A synthetic oscillatory network of transcriptional regulators
TL;DR: This work used three transcriptional repressor systems that are not part of any natural biological clock to build an oscillating network, termed the repressilator, in Escherichia coli, which periodically induces the synthesis of green fluorescent protein as a readout of its state in individual cells.
Journal ArticleDOI
PEST sequences and regulation by proteolysis
TL;DR: Recent experimental support for the hypothesis that polypeptide sequences enriched in proline, glutamic acid, serine, and threonine target proteins for rapid destruction is provided with a number of papers providing strong evidence that PEST regions serve as proteolytic signals.
Journal ArticleDOI
Recombinant protein expression in Escherichia coli.
TL;DR: Recent progress in the fundamental understanding of transcription, translation, and protein folding in E. coli, together with serendipitous discoveries and the availability of improved genetic tools are making this bacterium more valuable than ever for the expression of complex eukaryotic proteins.
Journal ArticleDOI
In vitro selection and evolution of functional proteins by using ribosome display.
Jozef Hanes,Andreas Plückthun +1 more
TL;DR: Libraries of native folded proteins can now be screened and made to evolve in a cell-free system without any transformation or constraints imposed by the host cell.
Journal ArticleDOI
Aminoacyl-tRNA synthesis.
Michael Ibba,Dieter Söll +1 more
TL;DR: Current knowledge of the biochemical, structural, and evolutionary facets of aminoacyl-tRNA synthesis is reviewed, mainly prompted by the advent of whole genome sequencing and the availability of vast body of structural data.
References
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Journal ArticleDOI
The ubiquitin-proteasome proteolytic pathway
TL;DR: Two studies clearly demonstrate that the ubiquitin-proteasome system is involved not only in complete destruction of its protein substrates, but also in limited proteolysis and posttranslational processing in which biologically active peptides or fragments are generated.
Journal ArticleDOI
Ubiquitin, proteasomes, and the regulation of intracellular protein degradation.
TL;DR: The complexity of the ubiquitin system is reflected in the broad range of processes it regulates; these include key steps in cell cycle progression, processing of foreign proteins for presentation by class I MHC molecules, and the control of cell proliferation.
Journal ArticleDOI
Regulation by proteolysis: energy-dependent proteases and their targets.
S Gottesman,M R Maurizi +1 more
TL;DR: A number of critical regulatory proteins in both prokaryotic and eukaryotic cells are subject to rapid, energy-dependent proteolysis, providing a mechanism by which the availability of a protein can be limited both temporally and spatially.
Journal ArticleDOI
Universality and structure of the N-end rule.
David K. Gonda,Andreas Bachmair,Andreas Bachmair,I Wünning,I Wünning,John W. Tobias,William S. Lane,Alexander Varshavsky,Alexander Varshavsky +8 more
TL;DR: In reticulocytes, distinct types of the N-end-recognizing activity are shown to be specific for three classes of primary destabilizing residues: basic (Arg, Lys, His), bulky hydrophobic (Phe, Leu, Trp, Tyr), and small uncharged (Ala, Ser, Thr).
Journal ArticleDOI
A tRNA-like structure is present in 10Sa RNA, a small stable RNA from Escherichia coli
TL;DR: Primer-extension analysis of 10Sa RNA extracted from a bacterial mutant with temperature-sensitive RNase P function revealed that the precursor to 10SaRNA (pre-10Sa RNA) is folded into a pre-tRNA-like structure in vivo such that it can be cleaved byRNase P to generate the 5' end of the mature 10 Sa RNA.