The hetero-hexameric nature of a chloroplast AAA+ FtsH protease contributes to its thermodynamic stability.

PloS One
Ofer MoldavskiGali Prag

Abstract

FtsH is an evolutionary conserved membrane-bound metalloprotease complex. While in most prokaryotes FtsH is encoded by a single gene, multiple FtsH genes are found in eukaryotes. Genetic and biochemical data suggest that the Arabidopsis chloroplast FtsH is a hetero-hexamer. This raises the question why photosynthetic organisms require a heteromeric complex, whereas in most bacteria a homomeric one is sufficient. To gain structural information of the possible complexes, the Arabidopsis FtsH2 (type B) and FtsH5 (type A) were modeled. An in silico study with mixed models of FtsH2/5 suggests that heteromeric hexamer structure with ratio of 4:2 is more likely to exists. Specifically, calculation of the buried surface area at the interfaces between neighboring subunits revealed that a hetero-complex should be thermodynamically more stable than a homo-hexamer, due to the presence of additional hydrophobic and hydrophilic interactions. To biochemically assess this model, we generated Arabidopsis transgenic plants, expressing epitope-tagged FtsH2 and immuno-purified the protein. Mass-spectrometry analysis showed that FtsH2 is associated with FtsH1, FtsH5 and FtsH8. Interestingly, we found that 'type B' subunits (FtsH2 and FtsH8) were 2-...Continue Reading

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Citations

Aug 21, 2012·The Plant Journal : for Cell and Molecular Biology·Deena K Kadirjan-KalbachKatherine W Osteryoung
Mar 28, 2016·Plant & Cell Physiology·Miho Yoshioka-Nishimura

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Methods Mentioned

BETA
transgenic
PCR
gel
electrophoresis
co-immunoprecipitation
reverse-phase chromatography

Software Mentioned

PyMol
Miner
Rasmol
Sequest
Pep
GENO3D
Refmac5
BLAST

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