Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
17
pubmed:dateCreated
1992-7-16
pubmed:abstractText
A variety of model presecretory proteins, proOmpF-Lpps, possessing different numbers of lysine residues (0, 2, and 4) as positively charged amino acid residues and different numbers of leucine residues (7, 8, and 9) as hydrophobic amino acid residues in their signal peptides were constructed. The effect of positive charges on the in vitro translocation efficiency markedly differed with the number of leucine residues. Positive charges were strongly required for translocation when the hydrophobic region comprised 7 or 8 leucine residues, whereas the translocation of proOmpF-Lpps possessing 9 leucine residues took place efficiently even in the absence of positive charges and the introduction of positive charges did not significantly enhance the translocation efficiency. The translocation of all the proOmpF-Lpps, including one possessing no positive charge, was ATP-, protonmotive force-, and SecA-dependent and accompanied by signal peptide cleavage, indicating that they are translocated via the usual secretory pathway. It is likely that the requirement of positive charges can be compensated for by a longer hydrophobic stretch in the functioning of the signal peptide.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases, http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Outer Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Transport Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Protein Precursors, http://linkedlifedata.com/resource/pubmed/chemical/Protein Sorting Signals, http://linkedlifedata.com/resource/pubmed/chemical/Protons, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/SecA protein, Bacteria, http://linkedlifedata.com/resource/pubmed/chemical/proOmpF-Lpp secretory protein...
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
267
pubmed:geneSymbol
ompF-lpp
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
12375-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:1318317-Adenosine Triphosphatases, pubmed-meshheading:1318317-Adenosine Triphosphate, pubmed-meshheading:1318317-Amino Acid Sequence, pubmed-meshheading:1318317-Bacterial Outer Membrane Proteins, pubmed-meshheading:1318317-Bacterial Proteins, pubmed-meshheading:1318317-Electrochemistry, pubmed-meshheading:1318317-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:1318317-Escherichia coli, pubmed-meshheading:1318317-Escherichia coli Proteins, pubmed-meshheading:1318317-Kinetics, pubmed-meshheading:1318317-Lipoproteins, pubmed-meshheading:1318317-Membrane Transport Proteins, pubmed-meshheading:1318317-Molecular Sequence Data, pubmed-meshheading:1318317-Plasmids, pubmed-meshheading:1318317-Protein Precursors, pubmed-meshheading:1318317-Protein Sorting Signals, pubmed-meshheading:1318317-Protons, pubmed-meshheading:1318317-Recombinant Proteins
pubmed:year
1992
pubmed:articleTitle
The requirement of a positive charge at the amino terminus can be compensated for by a longer central hydrophobic stretch in the functioning of signal peptides.
pubmed:affiliation
Institute of Applied Microbiology, University of Tokyo, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't