Linked Life Data

9268025

Source:http://linkedlifedata.com/resource/pubmed/id/9268025

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1997-9-18
pubmed:databankReference
pubmed:abstractText
The mgi1-4 and mgi2-1 mutants of the petite-negative yeast Kluyveromyces lactis have mutations in the beta- and alpha-subunits of the mitochondrial F1-ATPase, respectively. The mutants are respiratory competent but can form petites with deletions in mitochondrial DNA. In this study a cryptic nuclear mutation (lipB-1) was identified which, in combination with the mgi alleles, displays a synergistic respiratory-deficient phenotype on glycerol medium. The gene defined by the mutation was cloned and shown to encode a polypeptide of 332 amino acids with an N-terminal sequence characteristic of a mitochondrial targeting signal. The deduced protein shares 27% sequence identity with the product of the Escherichia coli lipB gene, which encodes a lipoyl-protein ligase involved in the attachment of lipoyl groups to lipoate-dependent apoproteins. A K. lactis strain carrying a disrupted lipB allele is severely compromised for growth on glycerol medium. The growth defect cannot be rescued by addition of lipoic acid, but cell growth can be restored on medium containing ethanol plus succinate. In addition, it was observed that lipB mutants of K. lactis, unlike the wild-type, are unable to utilize glycine as sole nitrogen source, indicating that activity of the glycine decarboxylase complex (GDC) is also affected. Taken together, these findings suggest that LIPB is the main determinant of the lipoyl-protein ligase activity required for lipoylation of enzymes such as alpha-ketoacid dehydrogenases and GDC.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0026-8925
pubmed:author
pubmed:issnType
Print
pubmed:volume
255
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
341-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:9268025-Amino Acid Sequence, pubmed-meshheading:9268025-Base Sequence, pubmed-meshheading:9268025-Cell Division, pubmed-meshheading:9268025-Cloning, Molecular, pubmed-meshheading:9268025-DNA, Mitochondrial, pubmed-meshheading:9268025-Ethanol, pubmed-meshheading:9268025-Fungal Proteins, pubmed-meshheading:9268025-Genes, Fungal, pubmed-meshheading:9268025-Glycine, pubmed-meshheading:9268025-Kluyveromyces, pubmed-meshheading:9268025-Mitochondria, pubmed-meshheading:9268025-Molecular Sequence Data, pubmed-meshheading:9268025-Mutation, pubmed-meshheading:9268025-Oxygen Consumption, pubmed-meshheading:9268025-Peptide Synthases, pubmed-meshheading:9268025-Proton-Translocating ATPases, pubmed-meshheading:9268025-Sequence Analysis, DNA, pubmed-meshheading:9268025-Sequence Homology, Amino Acid, pubmed-meshheading:9268025-Succinates, pubmed-meshheading:9268025-Succinic Acid
pubmed:year
1997
pubmed:articleTitle
Cloning and characterization of the lipoyl-protein ligase gene LIPB from the yeast Kluyveromyces lactis: synergistic respiratory deficiency due to mutations in LIPB and mitochondrial F1-ATPase subunits.
pubmed:affiliation
Molecular and Population Genetics Group, Research School of Biological Sciences, The Australian National University, Canberra City, ACT. chen@rsbs-central.anu.edu.au
pubmed:publicationType
Journal Article, Comparative Study