Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2002-3-20
pubmed:abstractText
The ammonium/methylammonium transport (Amt) proteins of enteric bacteria and their homologues, the methylammonium/ammonium permeases of Saccharomyces cerevisiae, are required for fast growth at very low concentrations of the uncharged species NH(3). For example, they are essential at low ammonium (NH(4)+ + NH(3)) concentrations under acidic conditions. Based on growth studies in batch culture, the Amt protein of Salmonella typhimurium (AmtB) cannot concentrate either NH(3) or NH(4)+ and this organism appears to have no means of doing so. We now show that S. typhimurium releases ammonium into the medium when grown on the alternative nitrogen source arginine and that outward diffusion of ammonium is enhanced by the activity of AmtB. The latter result indicates that AmtB acts bidirectionally. We also confirm a prediction that the AmtB protein would be required at pH 7.0 in ammonium-limited continuous culture, i.e., when the concentration of NH(3) is < or =50 nM. Together with our previous studies, current results are in accord with the view that Amt and methylammonium/ammonium permease proteins increase the rate of diffusion of the uncharged species NH(3) across the cytoplasmic membrane. These proteins are examples of protein facilitators for a gas.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/11891327-10748252, http://linkedlifedata.com/resource/pubmed/commentcorrection/11891327-10837267, http://linkedlifedata.com/resource/pubmed/commentcorrection/11891327-11214321, http://linkedlifedata.com/resource/pubmed/commentcorrection/11891327-11358367, http://linkedlifedata.com/resource/pubmed/commentcorrection/11891327-11486013, http://linkedlifedata.com/resource/pubmed/commentcorrection/11891327-1309519, http://linkedlifedata.com/resource/pubmed/commentcorrection/11891327-1937792, http://linkedlifedata.com/resource/pubmed/commentcorrection/11891327-5498410, http://linkedlifedata.com/resource/pubmed/commentcorrection/11891327-7012838, http://linkedlifedata.com/resource/pubmed/commentcorrection/11891327-728998, http://linkedlifedata.com/resource/pubmed/commentcorrection/11891327-8683567, http://linkedlifedata.com/resource/pubmed/commentcorrection/11891327-9234685, http://linkedlifedata.com/resource/pubmed/commentcorrection/11891327-9393691, http://linkedlifedata.com/resource/pubmed/commentcorrection/11891327-9433124, http://linkedlifedata.com/resource/pubmed/commentcorrection/11891327-9529885, http://linkedlifedata.com/resource/pubmed/commentcorrection/11891327-9618533, http://linkedlifedata.com/resource/pubmed/commentcorrection/11891327-9696779, http://linkedlifedata.com/resource/pubmed/commentcorrection/11891327-9861053
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:day
19
pubmed:volume
99
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3926-31
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Ammonium/methylammonium transport (Amt) proteins facilitate diffusion of NH3 bidirectionally.
pubmed:affiliation
Department of Plant and Microbial Biology, University of California, 111 Koshland Hall, 3102, Berkeley, CA 94720-3102, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.