Involvement of Deg5 protease in wounding-related disposal of PsbF apoprotein

Deg5 is a serine-type protease peripherally attached to luminal side of thylakoid membrane. Given the lack of knowledge concerning its function homozygous T-DNA insertion line depleted in Deg5 was prepared to study the functional importance of this protease in Arabidopsis thaliana. deg5 mutants disp...

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Published in:Plant physiology and biochemistry Vol. 49; no. 3; pp. 311 - 320
Main Authors: Luciński, Robert, Misztal, Lucyna, Samardakiewicz, Sławomir, Jackowski, Grzegorz
Format: Journal Article
Language:English
Published: Paris Elsevier Masson SAS 01-03-2011
Elsevier
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Summary:Deg5 is a serine-type protease peripherally attached to luminal side of thylakoid membrane. Given the lack of knowledge concerning its function homozygous T-DNA insertion line depleted in Deg5 was prepared to study the functional importance of this protease in Arabidopsis thaliana. deg5 mutants displayed a pleiotropic phenotype with regard to fourth whorl leaves of four-weeks old plants. The alterations involved an increased leaf area, reduced leaf thickness, reduced cross-sectional area of palisade mesophyll cells as well as changed chloroplast ultrastructure including lack of signs of entering the senescence phase (e.g. presence of much smaller plastoglobules) and the accumulation of large starch grains at the end of the dark period. It was shown that whereas PsbA, C and F apoproteins of photosystem II reaction center undergo an extensive disappearance in response to a set of brief stresses deg5 mutant was fully resistant to the disappearance of PsbF apoprotein which follows an exposition of leaves to wounding. Our results demonstrate that Deg5 is of seminal importance for normal plant development and degradation of PsbF which occurs following brief wounding. ► PsbA, C and F apoproteins undergo a disappearance in response to four brief stresses. ► Deg5 is responsible for wounding-related disposal of PsbF apoprotein. ► deg5 mutant displays changes in leaf morphology, anatomy and chloroplast ultrastructure.
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ISSN:0981-9428
1873-2690
DOI:10.1016/j.plaphy.2011.01.001