|
rdf:type |
|
|
lifeskim:mentions |
umls-concept:C0007630,
umls-concept:C0007641,
umls-concept:C0026882,
umls-concept:C0033684,
umls-concept:C0078638,
umls-concept:C0079429,
umls-concept:C0243144,
umls-concept:C0596988,
umls-concept:C0679058,
umls-concept:C0995754,
umls-concept:C1334043,
umls-concept:C1547699,
umls-concept:C2700640
|
|
pubmed:issue |
2
|
|
pubmed:dateCreated |
1996-1-11
|
|
pubmed:databankReference |
|
|
pubmed:abstractText |
The uptake of monosaccharides (glucose and xylose) and disaccharides (cellobiose and xylobiose) was evaluated in the Streptomyces lividans mutant strain 10-164. The pleiotropic mutation had no effect on glucose uptake; however, the Vmax of xylose uptake was decreased 10-fold as compared to the wild-type strain, S. lividans 1326, and the transport system of cellobiose and xylobiose, the putative inducers of the cellulase and xylanase genes, was completely abolished resulting in a cellulase/xylanase-negative mutant. An accumulation of xylose and glucose in culture media was observed when the mutant was grown on xylobiose and cellobiose, respectively. Cell-associated beta-glucosidase and low levels of extracellular beta-glucosidase were detected in both strains. When gluconolactone, a beta-glucosidase inhibitor, was added to the medium there was no uptake of cellobiose or release of glucose by the mutant strain, whereas the uptake of cellobiose by the wild-type strain was not significantly affected. It is thus proposed that the active transport system for cellobiose and xylobiose is affected in mutant strain 10-164. Glucose and xylose production from disaccharide hydrolysis are due to beta-glucosidase and beta-xylosidase activities, which sustain the growth of the mutant strain. Clones complementing the mutation were isolated from a gene bank constructed using mutant strain 10-164. The msiK gene codes for MsiK, a 40 kDa multiple sugar import protein, which belongs to the family of ATP-binding proteins. The mutation is located in the B site which is responsible for ATP binding. This protein probably provides energy to the xylose and disaccharide transport system as a result of the hydrolysis of ATP.
|
|
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 Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cellobiose,
http://linkedlifedata.com/resource/pubmed/chemical/Cellulase,
http://linkedlifedata.com/resource/pubmed/chemical/Disaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Gluconates,
http://linkedlifedata.com/resource/pubmed/chemical/Lactones,
http://linkedlifedata.com/resource/pubmed/chemical/Xylan Endo-1,3-beta-Xylosidase,
http://linkedlifedata.com/resource/pubmed/chemical/Xylose,
http://linkedlifedata.com/resource/pubmed/chemical/Xylosidases,
http://linkedlifedata.com/resource/pubmed/chemical/beta-Glucosidase,
http://linkedlifedata.com/resource/pubmed/chemical/beta-glucono-1,5-lactone,
http://linkedlifedata.com/resource/pubmed/chemical/xylobiose
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Jul
|
|
pubmed:issn |
0950-382X
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
17
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
367-77
|
|
pubmed:dateRevised |
2010-11-18
|
|
pubmed:meshHeading |
pubmed-meshheading:7494485-Adenosine Triphosphatases,
pubmed-meshheading:7494485-Adenosine Triphosphate,
pubmed-meshheading:7494485-Amino Acid Sequence,
pubmed-meshheading:7494485-Bacterial Proteins,
pubmed-meshheading:7494485-Base Sequence,
pubmed-meshheading:7494485-Biological Transport,
pubmed-meshheading:7494485-Carrier Proteins,
pubmed-meshheading:7494485-Cellobiose,
pubmed-meshheading:7494485-Cellulase,
pubmed-meshheading:7494485-Cloning, Molecular,
pubmed-meshheading:7494485-Disaccharides,
pubmed-meshheading:7494485-Enzyme Inhibitors,
pubmed-meshheading:7494485-Genes, Bacterial,
pubmed-meshheading:7494485-Gluconates,
pubmed-meshheading:7494485-Kinetics,
pubmed-meshheading:7494485-Lactones,
pubmed-meshheading:7494485-Molecular Sequence Data,
pubmed-meshheading:7494485-Mutation,
pubmed-meshheading:7494485-Sequence Analysis, DNA,
pubmed-meshheading:7494485-Sequence Homology, Amino Acid,
pubmed-meshheading:7494485-Streptomyces,
pubmed-meshheading:7494485-Xylan Endo-1,3-beta-Xylosidase,
pubmed-meshheading:7494485-Xylose,
pubmed-meshheading:7494485-Xylosidases,
pubmed-meshheading:7494485-beta-Glucosidase
|
|
pubmed:year |
1995
|
|
pubmed:articleTitle |
A cellulase/xylanase-negative mutant of Streptomyces lividans 1326 defective in cellobiose and xylobiose uptake is mutated in a gene encoding a protein homologous to ATP-binding proteins.
|
|
pubmed:affiliation |
Centre de Recherche en Microbiologie Appliquée, Institut Armand-Frappier, Université du Québec, Ville de Laval, Canada.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
