Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5530
pubmed:dateCreated
2001-7-27
pubmed:abstractText
Inorganic polyphosphate (polyP), a polymer of hundreds of phosphate (Pi) residues, accumulates in Escherichia coli in response to stresses, including amino acid starvation. Here we show that the adenosine 5'-triphosphate-dependent protease Lon formed a complex with polyP and degraded most of the ribosomal proteins, including S2, L9, and L13. Purified S2 also bound to polyP and formed a complex with Lon in the presence of polyP. Thus, polyP may promote ribosomal protein degradation by the Lon protease, thereby supplying the amino acids needed to respond to starvation.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/ATP-Dependent Proteases, http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases, http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Amino Acids, http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidase Clp, http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Heat-Shock Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Lon protein, E coli, http://linkedlifedata.com/resource/pubmed/chemical/Phosphotransferases (Phosphate..., http://linkedlifedata.com/resource/pubmed/chemical/Polyphosphates, http://linkedlifedata.com/resource/pubmed/chemical/Protease La, http://linkedlifedata.com/resource/pubmed/chemical/Ribosomal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Serine Endopeptidases, http://linkedlifedata.com/resource/pubmed/chemical/polyphosphate kinase, http://linkedlifedata.com/resource/pubmed/chemical/ribosomal protein L9, http://linkedlifedata.com/resource/pubmed/chemical/ribosomal protein S2
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0036-8075
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
293
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
705-8
pubmed:dateRevised
2007-3-19
pubmed:meshHeading
pubmed-meshheading:11474114-ATP-Dependent Proteases, pubmed-meshheading:11474114-Adaptation, Physiological, pubmed-meshheading:11474114-Adenosine Triphosphatases, pubmed-meshheading:11474114-Adenosine Triphosphate, pubmed-meshheading:11474114-Amino Acid Sequence, pubmed-meshheading:11474114-Amino Acids, pubmed-meshheading:11474114-Bacterial Proteins, pubmed-meshheading:11474114-Endopeptidase Clp, pubmed-meshheading:11474114-Escherichia coli, pubmed-meshheading:11474114-Escherichia coli Proteins, pubmed-meshheading:11474114-Heat-Shock Proteins, pubmed-meshheading:11474114-Molecular Sequence Data, pubmed-meshheading:11474114-Mutation, pubmed-meshheading:11474114-Phosphotransferases (Phosphate Group Acceptor), pubmed-meshheading:11474114-Polyphosphates, pubmed-meshheading:11474114-Protease La, pubmed-meshheading:11474114-Ribosomal Proteins, pubmed-meshheading:11474114-Ribosomes, pubmed-meshheading:11474114-Serine Endopeptidases
pubmed:year
2001
pubmed:articleTitle
Role of inorganic polyphosphate in promoting ribosomal protein degradation by the Lon protease in E. coli.
pubmed:affiliation
Department of Molecular Biotechnology, Graduate School of Advanced Sciences of Matter, Hiroshima University, 1-4-1 Kagamiyama, Hiroshima 739-8527, Japan. akuroda@hiroshima-u.ac.jp
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't