Expansion of the evolutionarily conserved network of J-domain proteins in the Arabidopsis mitochondrial import complex.

Plant Molecular Biology
Chetana TamadaddiChandan Sahi

Abstract

We report that discriminate interaction between the expanded mitochondrial chaperone network and variability in their expression might determine their functional specificities and impart robustness to mitochondrial import processes in plants. Mitochondrial Hsp70 (mtHsp70), the central component of the pre-sequence associated motor (PAM) complex, is crucial for the import of proteins to the mitochondrial matrix. Activity of mtHsp70 is regulated by a heterodimeric complex of two J-domain proteins (JDPs), Pam18 and Pam16. Compared to other eukaryotes, plants harbor multiple copies of these JDPs, which posit that plants have an increasingly complex mtHsp70: JDP network in their mitochondrial matrix. Here, we show that although highly similar in sequence, some of the plant JDPs are functionally different. Protein: protein interaction studies including yeast two-hybrid and Bimolecular Fluorescence Complementation revealed that while all the AtPam18s interacted with AtPam16s, the strengths of these promiscuous interactions are variable. Further, down-regulation of AtPAM16L affected seed germination, even in the presence of its seemingly identical paralog, AtPAM16. Knockdown of AtPAM16L caused reduction in mitochondrial number and dere...Continue Reading

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Methods Mentioned

BETA
transgenic
electrophoresis
PCR
Y2H
two-hybrid
Genotyping
confocal microscopy

Software Mentioned

SWISS
Multiple Align Show
Heatmapper
eFP browser
eFP
browser
MODEL
TAIR BLAST
PyMOL
Multalign interface

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