rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
15
|
pubmed:dateCreated |
2001-8-7
|
pubmed:abstractText |
Cellulose-binding modules (CBMs) of two extracellular matrix proteins, St15 and ShD, from the slime mold Dictyostelium discoideum were expressed in Escherichia coli. The expressed proteins were purified to > 98% purity by extracting inclusion bodies at pH 11.5 and refolding proteins at pH 7.5. The two refolded CBMs bound tightly to amorphous phosphoric acid swollen cellulose (PASC), but had a low affinity toward xylan. Neither protein exhibited cellulase activity. St15, the stalk-specific protein, had fourfold higher binding affinity toward microcrystalline cellulose (Avicel) than the sheath-specific ShD CBM. St15 is unusual in that it consists of a solitary CBM homologous to family IIa CBMs. Sequence analysis of ShD reveals three putative domains containing: (a) a C-terminal CBM homologous to family IIb CBMs; (b) a Pro/Thr-rich linker domain; and (c) a N-terminal Cys-rich domain. The biological functions and potential role of St15 and ShD in building extracellular matrices during D. discoideum development are discussed.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cellulase,
http://linkedlifedata.com/resource/pubmed/chemical/Cellulose,
http://linkedlifedata.com/resource/pubmed/chemical/Coloring Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Coomassie blue,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protozoan Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Rosaniline Dyes,
http://linkedlifedata.com/resource/pubmed/chemical/Salts
|
pubmed:status |
MEDLINE
|
pubmed:month |
Aug
|
pubmed:issn |
0014-2956
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
268
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
4334-45
|
pubmed:dateRevised |
2007-7-23
|
pubmed:meshHeading |
pubmed-meshheading:11488929-Amino Acid Sequence,
pubmed-meshheading:11488929-Animals,
pubmed-meshheading:11488929-Base Sequence,
pubmed-meshheading:11488929-Binding Sites,
pubmed-meshheading:11488929-Blotting, Western,
pubmed-meshheading:11488929-Cellulase,
pubmed-meshheading:11488929-Cellulose,
pubmed-meshheading:11488929-Cloning, Molecular,
pubmed-meshheading:11488929-Coloring Agents,
pubmed-meshheading:11488929-DNA, Complementary,
pubmed-meshheading:11488929-Dictyostelium,
pubmed-meshheading:11488929-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:11488929-Escherichia coli,
pubmed-meshheading:11488929-Extracellular Matrix,
pubmed-meshheading:11488929-Hydrogen-Ion Concentration,
pubmed-meshheading:11488929-Kinetics,
pubmed-meshheading:11488929-Models, Biological,
pubmed-meshheading:11488929-Molecular Sequence Data,
pubmed-meshheading:11488929-Polymerase Chain Reaction,
pubmed-meshheading:11488929-Protein Binding,
pubmed-meshheading:11488929-Protein Folding,
pubmed-meshheading:11488929-Protein Structure, Tertiary,
pubmed-meshheading:11488929-Proto-Oncogene Proteins,
pubmed-meshheading:11488929-Protozoan Proteins,
pubmed-meshheading:11488929-Recombinant Fusion Proteins,
pubmed-meshheading:11488929-Recombinant Proteins,
pubmed-meshheading:11488929-Rosaniline Dyes,
pubmed-meshheading:11488929-Salts,
pubmed-meshheading:11488929-Sequence Analysis, Protein,
pubmed-meshheading:11488929-Sequence Homology, Amino Acid
|
pubmed:year |
2001
|
pubmed:articleTitle |
Cellulose-binding modules from extracellular matrix proteins of Dictyostelium discoideum stalk and sheath.
|
pubmed:affiliation |
Department of Biological Sciences, Macquarie University, Sydney, NSW, Australia.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|