Linked Life Data

9611797

Source:http://linkedlifedata.com/resource/pubmed/id/9611797

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1998-7-7
pubmed:databankReference
pubmed:abstractText
Oral streptococci such as Streptococcus gordonii bind the abundant salivary enzyme alpha-amylase. This interaction may be important in dental plaque formation and metabolism, thus contributing to the initiation and progression of dental caries and periodontal disease, the two most common plaque-mediated diseases. The conjugative transposon Tn916 was used to insertionally inactivate gene(s) essential to the expression of amylase-binding components of S. gordonii Challis, and a mutant deficient in amylase-binding (Challis Tn1) was identified. While wild-type strains of S. gordonii released both 20 kDa and 82 kDa amylase-binding proteins into culture supernatants, Challis Tn1 expressed the 82 kDa but not the 20 kDa protein. The 20 kDa amylase-binding protein was isolated from culture supernatants of S. gordonii Challis by hydroxyapatite chromatography. A partially purified, functionally active 20 kDa protein was sequenced from blots, and the N-terminal sequence obtained was found to be DEP(A)TDAAT(R)NND. A novel strategy, based on the single-specific-primer polymerase chain reaction technique, enabled the gene inactivated by Tn916 to be cloned. Analysis of the resultant nucleotide sequence revealed an open reading frame of 585 bp, designated amylase-binding protein A (abpA), encoding a protein of 20 kDa (AbpA), immediately downstream from the insertion site of Tn916. This protein possessed a potential signal peptide followed by a region having identity with the N-terminal sequence of the 20 kDa amylase-binding protein. These results demonstrate the role of the 20 kDa protein in the binding of amylase to S. gordonii. Knowledge of the nature of amylase-binding proteins may provide a better understanding of the role of these proteins in the colonization of S. gordonii in the oral cavity.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1350-0872
pubmed:author
pubmed:issnType
Print
pubmed:volume
144 ( Pt 5)
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1223-33
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:9611797-Amino Acid Sequence, pubmed-meshheading:9611797-Amylases, pubmed-meshheading:9611797-Bacterial Outer Membrane Proteins, pubmed-meshheading:9611797-Bacterial Proteins, pubmed-meshheading:9611797-Base Sequence, pubmed-meshheading:9611797-Blotting, Western, pubmed-meshheading:9611797-Carrier Proteins, pubmed-meshheading:9611797-Cloning, Molecular, pubmed-meshheading:9611797-DNA Transposable Elements, pubmed-meshheading:9611797-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:9611797-Genes, Bacterial, pubmed-meshheading:9611797-Genetic Linkage, pubmed-meshheading:9611797-Humans, pubmed-meshheading:9611797-Molecular Sequence Data, pubmed-meshheading:9611797-Mutagenesis, Insertional, pubmed-meshheading:9611797-Polymerase Chain Reaction, pubmed-meshheading:9611797-Protein Binding, pubmed-meshheading:9611797-Saliva, pubmed-meshheading:9611797-Sequence Analysis, DNA, pubmed-meshheading:9611797-Streptococcus, pubmed-meshheading:9611797-Transformation, Bacterial, pubmed-meshheading:9611797-Trypsin
pubmed:year
1998
pubmed:articleTitle
Identification and analysis of a gene (abpA) encoding a major amylase-binding protein in Streptococcus gordonii.
pubmed:affiliation
Department of Oral Biology, School of Dental Medicine, State University, New York at Buffalo 14214, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't