Linked Life Data

15003532

Source:http://linkedlifedata.com/resource/pubmed/id/15003532

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pubmed-article:15003532pubmed:dateCreated2004-3-8lld:pubmed
pubmed-article:15003532pubmed:abstractTextAll three tryptophan residues in alpha-subunit of mitochondrial processing peptidase (MPP) were subsequently substituted. While substitutions of Trp223 led to misfolded non-functional protein, mutations of Trp147 and/or Trp481 did not affect the enzyme processing activity. Thus, fluorescence properties of the mutants with fewer tryptophans were used for observation of both alpha-MPP domain translocation and visualization of conformational changes in the interdomain linker evoked by substrate. We found that in the presence of substrate the C-terminal penultimate Trp481 was approaching Trp223, which is localized at the border of N-terminal domain and interdomain linker. Also, excision of the alpha-MPP C-terminal 30 amino acid residues (DeltaC30) led to a complete loss of protein function. Even shorter deletions of the alpha-MPP C-terminus destabilized the protein slightly (DeltaC2) or dramatically (DeltaC17). It suggests that the extreme C-terminus of alpha-MPP provides mechanical support to the C-terminal domain during its extensive conformational change accompanying the substrate recognition process.lld:pubmed
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pubmed-article:15003532pubmed:volume316lld:pubmed
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pubmed-article:15003532pubmed:authorsCompleteYlld:pubmed
pubmed-article:15003532pubmed:pagination211-7lld:pubmed
pubmed-article:15003532pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:15003532pubmed:year2004lld:pubmed
pubmed-article:15003532pubmed:articleTitleSubstrate evokes translocation of both domains in the mitochondrial processing peptidase alpha-subunit during which the C-terminus acts as a stabilizing element.lld:pubmed
pubmed-article:15003532pubmed:affiliationInstitute of Microbiology, Academy of Sciences of the Czech Republic, Videnska 1083, 142 20 Prague 4, Czech Republic. janata@biomed.cas.czlld:pubmed
pubmed-article:15003532pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:15003532pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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