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A functional core of the mitochondrial genome maintenance protein Mgm101p in Saccharomyces cerevisiae determined with a temperature-conditional allele

Zuo, Xiaoming; Xue, Donghua; Li, Nan; Clark-Walker, George

Description

Analysis of Mgm101p isolated from mitochondria shows that the mature protein of 27.6 kDa lacks 22 amino acids from the N-terminus. This mitochondrial targeting sequence has been incorporated in the design of oligonucleotides used to determine a functional core of Mgm101p. Progressive deletions, although retaining the targeting sequence, reveal that 76 N-terminal and six C-terminal amino acids of Mgm101p can be removed without altering the ability to complement an mgm101-1ts...[Show more]

dc.contributor.authorZuo, Xiaoming
dc.contributor.authorXue, Donghua
dc.contributor.authorLi, Nan
dc.contributor.authorClark-Walker, George
dc.date.accessioned2015-12-10T22:27:53Z
dc.identifier.issn1567-1356
dc.identifier.urihttp://hdl.handle.net/1885/54394
dc.description.abstractAnalysis of Mgm101p isolated from mitochondria shows that the mature protein of 27.6 kDa lacks 22 amino acids from the N-terminus. This mitochondrial targeting sequence has been incorporated in the design of oligonucleotides used to determine a functional core of Mgm101p. Progressive deletions, although retaining the targeting sequence, reveal that 76 N-terminal and six C-terminal amino acids of Mgm101p can be removed without altering the ability to complement an mgm101-1ts temperature-sensitive mutant. However, this active core is unable to complement mgm101 null mutants, suggesting that the Mgm101p might need to form a dimer or multimer to be functional in vivo. The active core, enriched in basic residues, contains 165 amino acids with a pI of 9.2. Alignment with 22 Mgm101p sequences from other lower eukaryotes shows that a number of amino acids are highly conserved in this region. Random mutagenesis confirms that certain critical amino acids required for function are invariant across the 23 proteins. Searches in the PFAM database revealed a low level of structural similarity between the active core and the Rad52 protein family.
dc.publisherBlackwell Publishing Ltd
dc.sourceFEMS Yeast Research
dc.subjectKeywords: amino acid; dimer; fungal protein; polymer; protein Mgm101p; Rad52 protein; unclassified drug; allele; amino acid sequence; amino terminal sequence; article; carboxy terminal sequence; controlled study; dimerization; eukaryote; gene deletion; gene sequenc Functional core; Mgm101p; Mutagenesis; Signal peptide
dc.titleA functional core of the mitochondrial genome maintenance protein Mgm101p in Saccharomyces cerevisiae determined with a temperature-conditional allele
dc.typeJournal article
local.description.notesImported from ARIES
local.identifier.citationvolume7
dc.date.issued2007
local.identifier.absfor060107 - Enzymes
local.identifier.absfor060199 - Biochemistry and Cell Biology not elsewhere classified
local.identifier.ariespublicationu9204316xPUB299
local.type.statusPublished Version
local.contributor.affiliationZuo, Xiaoming, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationXue, Donghua, Northeast Normal University
local.contributor.affiliationLi, Nan, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationClark-Walker, George, College of Medicine, Biology and Environment, ANU
local.description.embargo2037-12-31
local.bibliographicCitation.startpage131
local.bibliographicCitation.lastpage140
local.identifier.doi10.1111/j.1567-1364.2006.00141.x
dc.date.updated2015-12-09T09:44:27Z
local.identifier.scopusID2-s2.0-33846322608
CollectionsANU Research Publications

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