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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
9
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pubmed:dateCreated |
1989-11-17
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pubmed:databankReference | |
pubmed:abstractText |
The complete nucleotide sequence of the xynA gene coding for a xylanase (XYLA) expressed by Pseudomonas fluorescens subspecies cellulosa, has been determined. The structural gene consists of an open reading frame of 1833 bp followed by a TAA stop codon. Confirmation of the nucleotide sequence was obtained by comparing the predicted amino acid sequence with that derived by N-terminal analysis of purified forms of the xylanase. The signal peptide present at the N terminus of mature XYLA closely resembles signal peptides of other secreted proteins. Truncated forms of the xylanase gene, in which the sequence encoding the N-terminal signal peptide had been deleted, still expressed coli. XYLA contains domains which are homologous to an endoglucanase expressed by the same organism. These structures include serine-rich sequences. Bal31 deletions of xynA revealed the extent to which these conserved sequences, in XYLA, were essential for xylanase activity. Downstream of the TAA stop codon is a G + C-rich region of dyad symmetry (delta G = 24 kcal) characteristic of E. coli Rho-independent transcription terminators.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cellulase,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoside Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Sorting Signals,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Serine,
http://linkedlifedata.com/resource/pubmed/chemical/Xylan Endo-1,3-beta-Xylosidase
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0950-382X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
3
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1211-9
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:2507868-Amino Acid Sequence,
pubmed-meshheading:2507868-Base Sequence,
pubmed-meshheading:2507868-Cellulase,
pubmed-meshheading:2507868-Cloning, Molecular,
pubmed-meshheading:2507868-Glycoside Hydrolases,
pubmed-meshheading:2507868-Molecular Sequence Data,
pubmed-meshheading:2507868-Mutation,
pubmed-meshheading:2507868-Protein Processing, Post-Translational,
pubmed-meshheading:2507868-Protein Sorting Signals,
pubmed-meshheading:2507868-Pseudomonas fluorescens,
pubmed-meshheading:2507868-Recombinant Proteins,
pubmed-meshheading:2507868-Restriction Mapping,
pubmed-meshheading:2507868-Sequence Homology, Nucleic Acid,
pubmed-meshheading:2507868-Serine,
pubmed-meshheading:2507868-Xylan Endo-1,3-beta-Xylosidase
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pubmed:year |
1989
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pubmed:articleTitle |
Conserved serine-rich sequences in xylanase and cellulase from Pseudomonas fluorescens subspecies cellulosa: internal signal sequence and unusual protein processing.
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pubmed:affiliation |
Department of Agricultural Biochemistry and Nutrition, University of Newcastle upon Tyne, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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