Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
1988-1-14
pubmed:abstractText
Overexpression of plasmid-coded PBP 3 was analyzed in strains harboring ftsA, ftsH, pbpB (ftsI), ftsQ, ftsZ, or recA441 (Tif) mutations. Higher cellular levels of PBP 3, the pbpB gene product, could not restore septum formation of ftsA, ftsQ, ftsZ, and recA (Tif) mutants at 42 degrees C. However, filamentation in strains harboring pbpB and ftsH mutations was fully suppressed by PBP 3 overexpression. Additional observations indicated that the Y16 (ftsH) strain, not transformed with the PBP 3-overproducing plasmid, had no detectable PBP 3 in envelopes after incubation at the restrictive temperature. These results suggest that suppression of filamentation of fts strains overexpressing wild-type cell division proteins after the shift to the restrictive temperature can be a useful strategy to demonstrate in vivo interactions of cell division gene products.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/3316193-1097423, http://linkedlifedata.com/resource/pubmed/commentcorrection/3316193-1104589, http://linkedlifedata.com/resource/pubmed/commentcorrection/3316193-14907713, http://linkedlifedata.com/resource/pubmed/commentcorrection/3316193-3011758, http://linkedlifedata.com/resource/pubmed/commentcorrection/3316193-3017915, http://linkedlifedata.com/resource/pubmed/commentcorrection/3316193-3025556, http://linkedlifedata.com/resource/pubmed/commentcorrection/3316193-319999, http://linkedlifedata.com/resource/pubmed/commentcorrection/3316193-326764, http://linkedlifedata.com/resource/pubmed/commentcorrection/3316193-338600, http://linkedlifedata.com/resource/pubmed/commentcorrection/3316193-345275, http://linkedlifedata.com/resource/pubmed/commentcorrection/3316193-3531167, http://linkedlifedata.com/resource/pubmed/commentcorrection/3316193-383579, http://linkedlifedata.com/resource/pubmed/commentcorrection/3316193-388439, http://linkedlifedata.com/resource/pubmed/commentcorrection/3316193-3894005, http://linkedlifedata.com/resource/pubmed/commentcorrection/3316193-3894330, http://linkedlifedata.com/resource/pubmed/commentcorrection/3316193-4565754, http://linkedlifedata.com/resource/pubmed/commentcorrection/3316193-4583216, http://linkedlifedata.com/resource/pubmed/commentcorrection/3316193-6337993, http://linkedlifedata.com/resource/pubmed/commentcorrection/3316193-6343351, http://linkedlifedata.com/resource/pubmed/commentcorrection/3316193-6365891, http://linkedlifedata.com/resource/pubmed/commentcorrection/3316193-6450748, http://linkedlifedata.com/resource/pubmed/commentcorrection/3316193-7009576, http://linkedlifedata.com/resource/pubmed/commentcorrection/3316193-7025060, http://linkedlifedata.com/resource/pubmed/commentcorrection/3316193-7030331, http://linkedlifedata.com/resource/pubmed/commentcorrection/3316193-773686
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Acyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins, http://linkedlifedata.com/resource/pubmed/chemical/FtsI protein, E coli, http://linkedlifedata.com/resource/pubmed/chemical/Hexosyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes, http://linkedlifedata.com/resource/pubmed/chemical/Muramoylpentapeptide..., http://linkedlifedata.com/resource/pubmed/chemical/Penicillin-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Peptidoglycan Glycosyltransferase, http://linkedlifedata.com/resource/pubmed/chemical/Peptidyl Transferases
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9193
pubmed:author
pubmed:issnType
Print
pubmed:volume
169
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5776-81
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:3316193-Acyltransferases, pubmed-meshheading:3316193-Bacterial Proteins, pubmed-meshheading:3316193-Carrier Proteins, pubmed-meshheading:3316193-Cell Division, pubmed-meshheading:3316193-Escherichia coli, pubmed-meshheading:3316193-Escherichia coli Proteins, pubmed-meshheading:3316193-Genes, Bacterial, pubmed-meshheading:3316193-Hexosyltransferases, pubmed-meshheading:3316193-Multienzyme Complexes, pubmed-meshheading:3316193-Muramoylpentapeptide Carboxypeptidase, pubmed-meshheading:3316193-Mutation, pubmed-meshheading:3316193-Penicillin-Binding Proteins, pubmed-meshheading:3316193-Peptidoglycan Glycosyltransferase, pubmed-meshheading:3316193-Peptidyl Transferases, pubmed-meshheading:3316193-Plasmids, pubmed-meshheading:3316193-Temperature, pubmed-meshheading:3316193-Transformation, Bacterial
pubmed:year
1987
pubmed:articleTitle
In vivo cell division gene product interactions in Escherichia coli K-12.
pubmed:affiliation
Departamento de Biofísica e Radiobiologia, Universidade Federal de Pernambuco-CCB, Cidade Universitária, Recife, Brazil.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't