AtDeg2 – a chloroplast protein with dual protease/chaperone activity
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Date
2014-07-09
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Polskie Towarzystwo Botaniczne
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Abstract
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.
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Keywords
AtDeg2, chaperone, chloroplast, hexamer, protease, PDZ domain
Citation
Acta Soc Bot Pol 83(3):169–174, 2014