AtDeg2 - a chloroplast protein with dual protease/chaperone activity

• Autorzy: Jagodzik P. , Adamiec M. , Jackowski G.
• Języki publikacji: EN

Abstrakty

EN

Chloroplast 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.

Słowa kluczowe

EN

chloroplast protein; protease; proteolytic enzyme; chaperone; enzyme activity; chloroplast; PDZ domain

• Wydawca: -
• Czasopismo: Acta Societatis Botanicorum Poloniae
• Rocznik: 2014
• Tom: 83
• Numer: 3
• Opis fizyczny: p.169-174,fig.,ref.

Twórcy

autor

Jagodzik P.

• Institute of Experimental Biology, Adam Mickiewicz University, Umultowska 89, 61-614 Poznan, Poland

autor

Adamiec M.

• Institute of Experimental Biology, Adam Mickiewicz University, Umultowska 89, 61-614 Poznan, Poland

autor

Jackowski G.

• Institute of Experimental Biology, Adam Mickiewicz University, Umultowska 89, 61-614 Poznan, Poland

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Identyfikatory

DOI

10.5586/asbp.2014.018