Statements in which the resource exists as a subject.
PredicateObject
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
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