Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
1988-12-20
pubmed:abstractText
We compared the secretion of a Bacillus subtilis endo-beta-1,4-glucanase (EC 3.2.1.4) in B. subtilis and of the product from the cloned gene (pC6.3) expressed in Escherichia coli. The cloned enzyme has been isolated previously as the 52.2-kilodalton (kDa) species predicted from the gene sequence (R. M. MacKay, A. Lo, G. Willick, M. Zuker, S. Baird, M. Dove, F. Moranelli, and V. Seligy, Nucleic Acids Res., 14:9159-9170, 1986); this 52.2-kDa species is then converted to an active 35.8-kDa species. The 35.8-kDa species has a segment removed from the COOH terminus. Endoglucanase products were identified by use of an antibody directed to the 35.8-kDa enzyme. Time course studies of the secretion in B. subtilis showed that the enzyme was first secreted as a 52.2-kDa proenzyme. This was cleaved progressively to a product of about 32 kDa. Time course analysis of the expression of the cloned product from pC6.3 in E. coli showed that about 70% of the endoglucanase activity was found extracellularly. Analysis of active products from three deletion clones showed that the expression pattern of the endoglucanase was not affected by removal of the transcription termination signal and that neither expression nor secretion was substantially altered by removal of a region coding for up to 163 residues of the carboxyl terminus.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/3142357-3003033, http://linkedlifedata.com/resource/pubmed/commentcorrection/3142357-3011754, http://linkedlifedata.com/resource/pubmed/commentcorrection/3142357-3024130, http://linkedlifedata.com/resource/pubmed/commentcorrection/3142357-3106328, http://linkedlifedata.com/resource/pubmed/commentcorrection/3142357-368040, http://linkedlifedata.com/resource/pubmed/commentcorrection/3142357-388439, http://linkedlifedata.com/resource/pubmed/commentcorrection/3142357-4594427, http://linkedlifedata.com/resource/pubmed/commentcorrection/3142357-4922220, http://linkedlifedata.com/resource/pubmed/commentcorrection/3142357-4954367, http://linkedlifedata.com/resource/pubmed/commentcorrection/3142357-5432063, http://linkedlifedata.com/resource/pubmed/commentcorrection/3142357-6182447, http://linkedlifedata.com/resource/pubmed/commentcorrection/3142357-6310323, http://linkedlifedata.com/resource/pubmed/commentcorrection/3142357-6313630, http://linkedlifedata.com/resource/pubmed/commentcorrection/3142357-6447703, http://linkedlifedata.com/resource/pubmed/commentcorrection/3142357-7108955
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0099-2240
pubmed:author
pubmed:issnType
Print
pubmed:volume
54
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2287-92
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Bacillus subtilis beta-1,4-endoglucanase products from intact and truncated genes are secreted into the extracellular medium by Escherichia coli.
pubmed:affiliation
Division of Biological Sciences, National Research Council of Canada, Ottawa, Ontario.
pubmed:publicationType
Journal Article