Please use this identifier to cite or link to this item: https://hdl.handle.net/10593/14772
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dc.contributor.authorJagodzik, Przemysław-
dc.contributor.authorAdamiec, Małgorzata-
dc.contributor.authorJackowski, Grzegorz-
dc.date.accessioned2016-06-28T08:38:53Z-
dc.date.available2016-06-28T08:38:53Z-
dc.date.issued2014-07-09-
dc.identifier.citationActa Soc Bot Pol 83(3):169–174, 2014pl_PL
dc.identifier.issn0001-6977-
dc.identifier.urihttp://hdl.handle.net/10593/14772-
dc.description.abstractChloroplast protease AtDeg2 (an ATP-independent serine endopeptidase) is cytosolically synthesized as a precursor, which is imported into the chloroplast stroma and deprived of its transit peptide. Then the mature protein undergoes routing to its functional location at the stromal side of thylakoid membrane. In its linear structure AtDeg2 molecule contains the protease domain with catalytic triad (HDS) and two PDZ domains (PDZ1 and PDZ2). In vivo AtDeg2 most probably exists as a supposedly inactive haxamer, which may change its oligomeric stage to form active 12-mer, or 24-mer. AtDeg2 has recently been demonstrated to exhibit dual protease/chaperone function. This review is focused on the current awareness with regard to AtDeg2 structure and functional significance.pl_PL
dc.language.isopolpl_PL
dc.publisherPolskie Towarzystwo Botanicznepl_PL
dc.rightsinfo:eu-repo/semantics/openAccesspl_PL
dc.subjectAtDeg2pl_PL
dc.subjectchaperonepl_PL
dc.subjectchloroplastpl_PL
dc.subjecthexamerpl_PL
dc.subjectproteasepl_PL
dc.subjectPDZ domainpl_PL
dc.titleAtDeg2 – a chloroplast protein with dual protease/chaperone activitypl_PL
dc.typeArtykułpl_PL
Appears in Collections:Artykuły naukowe (WB)

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