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10.1042/BCJ20160535 http://scihub22266oqcxt.onion/10.1042/BCJ20160535 C5095901!5095901!27422783     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Biochem+J 2016 ; 473 (18): 2813-29 Nephropedia Template TP {{tp|p=27422783|t=2016. Import of a major mitochondrial enzyme depends on synergy between two distinct helices of its presequence |pdf=|usr=}}{{27422783}} gab.com Text Import of a major mitochondrial enzyme depends on synergy between two distinct helices of its presequence JO: Biochem J http://www.kidney.de/pget.php?&tw=1&pmid=27422783 #FOAvip Mammalian glutamate dehydrogenase (GDH), a nuclear-encoded enzyme central to cellular metabolism, is among the most abundant mitochondrial proteins (constituting up to 10% of matrix proteins). To attain such high levels, GDH depends on very efficient mitochondrial targeting that, for human isoenzymes hGDH1 and hGDH2, is mediated by an unusually long cleavable presequence (N53). Here, we studied the mitochondrial transport of these proteins using isolated yeast mitochondria and human cell lines. We found that both hGDHs were very rapidly imported and processed in isolated mitochondria, with their presequences (N53) alone being capable of directing non-mitochondrial proteins into mitochondria. These presequences were predicted to form two ? helices (?1: N 1?10; ?2: N 16?32) separated by loops. Selective deletion of the ?1 helix abolished the mitochondrial import of hGDHs. While the ?1 helix alone had a very weak hGDH mitochondrial import capacity, it could direct efficiently non-mitochondrial proteins into mitochondria. In contrast, the ?2 helix had no autonomous mitochondrial-targeting capacity. A peptide consisting of ?1 and ?2 helices without intervening sequences had GDH transport efficiency comparable with that of N53. Mutagenesis of the cleavage site blocked the intra-mitochondrial processing of hGDHs, but did not affect their mitochondrial import. Replacement of all three positively charged N-terminal residues (Arg3, Lys7 and Arg13) by Ala abolished import. We conclude that the synergistic interaction of helices ?1 and ?2 is crucial for the highly efficient import of hGDHs into mitochondria. Twit Text FOAVip Import of a major mitochondrial enzyme depends on synergy between two distinct helices of its presequence ????Biochem J http://www.kidney.de/pget.php?&tw=1&pmid=27422783 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27422783 #FOAvip English Wikipedia <ref>{{Cite pmid|27422783}}</ref> Import of a major mitochondrial enzyme depends on synergy between two distinct helices of its presequence #MMPMID27422783 Kalef-Ezra E; Kotzamani D; Zaganas I; Katrakili N; Plaitakis A; Tokatlidis K Biochem J 2016[Sep]; 473 (18): 2813-29 PMID27422783show ga Mammalian glutamate dehydrogenase (GDH), a nuclear-encoded enzyme central to cellular metabolism, is among the most abundant mitochondrial proteins (constituting up to 10% of matrix proteins). To attain such high levels, GDH depends on very efficient mitochondrial targeting that, for human isoenzymes hGDH1 and hGDH2, is mediated by an unusually long cleavable presequence (N53). Here, we studied the mitochondrial transport of these proteins using isolated yeast mitochondria and human cell lines. We found that both hGDHs were very rapidly imported and processed in isolated mitochondria, with their presequences (N53) alone being capable of directing non-mitochondrial proteins into mitochondria. These presequences were predicted to form two ? helices (?1: N 1?10; ?2: N 16?32) separated by loops. Selective deletion of the ?1 helix abolished the mitochondrial import of hGDHs. While the ?1 helix alone had a very weak hGDH mitochondrial import capacity, it could direct efficiently non-mitochondrial proteins into mitochondria. In contrast, the ?2 helix had no autonomous mitochondrial-targeting capacity. A peptide consisting of ?1 and ?2 helices without intervening sequences had GDH transport efficiency comparable with that of N53. Mutagenesis of the cleavage site blocked the intra-mitochondrial processing of hGDHs, but did not affect their mitochondrial import. Replacement of all three positively charged N-terminal residues (Arg3, Lys7 and Arg13) by Ala abolished import. We conclude that the synergistic interaction of helices ?1 and ?2 is crucial for the highly efficient import of hGDHs into mitochondria. äImport of a major mitochondrial enzyme depends on synergy between two (epmc).pdf DeepDyve Pubget Overpricing