Electronic Resource
A functional core of the mitochondrial genome maintenance protein Mgm101p in Saccharomyces cerevisiae determined with a temperature-conditional allele
| العنوان: | A functional core of the mitochondrial genome maintenance protein Mgm101p in Saccharomyces cerevisiae determined with a temperature-conditional allele |
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| المؤلفون: | Zuo, Xiaoming, Xue, Donghua, Li, Nan, Clark-Walker, George |
| المصدر: | FEMS Yeast Research |
| بيانات النشر: | Blackwell Publishing Ltd 2007 |
| نوع الوثيقة: | Electronic Resource |
| مستخلص: | 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 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. |
| مصطلحات الفهرس: | Keywords: 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, Journal article |
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| الاتاحة: | Open access content. Open access content |
| Other Numbers: | AUANP oai:openresearch-repository.anu.edu.au:1885/54394 1567-1356 1291778581 |
| المصدر المساهم: | AUSTRALIAN NAT UNIV - PRINT REPOSITORY From OAIster®, provided by the OCLC Cooperative. |
| رقم الانضمام: | edsoai.on1291778581 |
| قاعدة البيانات: | OAIster |
| الوصف غير متاح. |