Abstract
Mutations in the beta-lactamase structural gene that alter the signal peptide were used to study secretion into the periplasm of Salmonella typhimurium. Processing and cellular location of mutant gene products were followed by pulse-chase and cell-fractionation experiments and by trypsin accessibility in intact and lysed spheroplasts. The precursor proteins examined never appear as a free species in the periplasm. Two of the signal-sequence mutants accumulate a precursor form that is trypsin-accessible in intact spheroplasts; the precursors synthesized by the remaining mutants resemble wild-type in that they remain trypsin-inaccessible. One of the latter mutants does produce mature protein, but at a very reduced rate. It thus appears that signal-sequence mutations can affect more than one step in the secretion process, and that processing of the signal peptide is not required for the protein to be translocated (at least partially) across the inner membrane.
Keywords
BiologySalmonellaSecretionSequence (biology)GeneticsSignal peptideMutationEnterobacteriaceaeMicrobiologyGeneEscherichia coliPeptide sequenceBacteriaBiochemistry
MeSH Terms
Amino Acid SequenceBase SequenceBiological TransportGenesMutationPeptidesPhenylethyl AlcoholProtein PrecursorsProtein ProcessingPost-TranslationalProtein Sorting SignalsSalmonella typhimuriumStructure-Activity Relationshipbeta-Lactamases
Affiliated Institutions
Related Publications
Resistance to Salmonellosis in the Chicken Is Linked to<i>NRAMP1</i>and <i>TNC</i>
Natural resistance to infection with Salmonella typhimurium in mice is controlled by two major loci, Bcg and Lps, located on mouse chromosomes 1 and 4, respectively. Both Bcg an...
Expert system for predicting protein localization sites in gram‐negative bacteria
Abstract We have developed an expert system that makes use of various kinds of knowledge organized as “if‐then” rules for predicting protein localization sites in Gram‐negative ...
The ins and outs of virulence gene expression: Mg2+ as a regulatory signal
The facultative intracellular pathogen Salmonella enterica serovar Typhimurium faces multiple environments during infection, including different cell types as well as extracellu...
SignalP 6.0 predicts all five types of signal peptides using protein language models
Signal peptides (SPs) are short amino acid sequences that control protein secretion and translocation in all living organisms. SPs can be predicted from sequence data, but exist...
Hepatocyte growth factor is a preferred <i>in vitro</i> substrate for human hepsin, a membrane-anchored serine protease implicated in prostate and ovarian cancers
Hepsin is a membrane-anchored, trypsin-like serine protease with prominent expression in the human liver and tumours of the prostate and ovaries. To better understand the biolog...
Publication Info
- Year
- 1982
- Type
- article
- Volume
- 30
- Issue
- 3
- Pages
- 903-914
- Citations
- 121
- Access
- Closed
External Links
Social Impact
Altmetric
PlumX Metrics
Social media, news, blog, policy document mentions
Citation Metrics
121
OpenAlex
1
Influential
101
CrossRef
Cite This
Douglas Koshland,
Robert T. Sauer,
David Botstein
(1982).
Diverse effects of mutations in the signal sequence on the secretion of β-lactamase in Salmonella typhimurium.
Cell
, 30
(3)
, 903-914.
https://doi.org/10.1016/0092-8674(82)90295-1
Identifiers
- DOI
- 10.1016/0092-8674(82)90295-1
- PMID
- 6183007