Linked Life Data

14872322

Source:http://linkedlifedata.com/resource/pubmed/id/14872322

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2004-6-15
pubmed:databankReference
pubmed:abstractText
In response to osmotic stress, the halophilic, Gram-positive bacterium Marinococcus halophilus accumulates compatible solutes either by de novo synthesis or by uptake from the medium. To characterize transport systems responsible for the uptake of compatible solutes, a plasmid-encoded gene bank of M. halophilus was transferred into the transport-deficient strain Escherichia coli MKH13, and two genes were cloned by functional complementation required for ectoine and glycine betaine transport. The ectoine transporter is encoded by an open reading frame of 1,578 bp named ectM. The gene ectM encodes a putative hydrophobic, 525-residue protein, which shares significant identity to betaine-carnetine-choline transporters (BCCTs). The transporter responsible for the uptake of glycine betaine in M. halophilus is encoded by an open reading frame of 1,482 bp called betM. The potential, hydrophobic BetM protein consists of 493 amino acid residues and belongs, like EctM, to the BCCT family. The affinity of whole cells of E. coli MKH13 for ectoine (Ks =1.6 microM) and betaine (Ks = 21.8 microM) was determined, suggesting that EctM and BetM exhibit a high affinity for their substrates. An elevation of the salinity in the medium resulted in an increased uptake of ectoine via EctM and glycine betaine via BetM in E. coli MKH13 cells, demonstrating that both systems are osmoregulated.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1431-0651
pubmed:author
pubmed:copyrightInfo
Copyright 2004 Springer-Verlag
pubmed:issnType
Print
pubmed:volume
8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
175-84
pubmed:dateRevised
2006-5-1
pubmed:meshHeading
pubmed-meshheading:14872322-Amino Acid Sequence, pubmed-meshheading:14872322-Amino Acids, Diamino, pubmed-meshheading:14872322-Bacterial Proteins, pubmed-meshheading:14872322-Betaine, pubmed-meshheading:14872322-Biological Transport, Active, pubmed-meshheading:14872322-Cloning, Molecular, pubmed-meshheading:14872322-DNA, Bacterial, pubmed-meshheading:14872322-Escherichia coli, pubmed-meshheading:14872322-Genes, Bacterial, pubmed-meshheading:14872322-Gram-Positive Bacteria, pubmed-meshheading:14872322-Kinetics, pubmed-meshheading:14872322-Membrane Transport Proteins, pubmed-meshheading:14872322-Molecular Sequence Data, pubmed-meshheading:14872322-Osmotic Pressure, pubmed-meshheading:14872322-Plasmids, pubmed-meshheading:14872322-Recombinant Proteins, pubmed-meshheading:14872322-Restriction Mapping, pubmed-meshheading:14872322-Sequence Homology, Amino Acid
pubmed:year
2004
pubmed:articleTitle
Marinococcus halophilus DSM 20408T encodes two transporters for compatible solutes belonging to the betaine-carnitine-choline transporter family: identification and characterization of ectoine transporter EctM and glycine betaine transporter BetM.
pubmed:affiliation
Institut für Mikrobiologie und Biotechnologie, Rheinische Friedrich-Wilhelms Universität, Meckenheimer Allee 168, 53115 Bonn, Germany.
pubmed:publicationType
Journal Article