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

Tamadaddi, Chetana; Sagar, Vinay; Verma, Amit; Afsal, Fathima; Sahi, Chandan

doi:10.1007/s11103-020-01095-8

Cited by 10 publications

(10 citation statements)

References 60 publications

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“…In plants, J-domain proteins have been reported to localize in different subcellular compartments and participate in various biological processes. A previous study showed that AtDjC5 (also named AtPam18-3) mainly exists in mitochondria [ 55 ]. However, in this study, we found that AtDjC5 showed a partial overlap with the ER maker ( Figure 4 A), indicating that AtDjC5 possibly has multiple subcellular localization.…”

Section: Discussionmentioning

confidence: 99%

The Arabidopsis J-Protein AtDjC5 Facilitates Thermotolerance Likely by Aiding in the ER Stress Response

Shen

Wang

Shang

et al. 2022

IJMS

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AtDjC5 belongs to the J-protein family in Arabidopsis thaliana. Its biological functions remain unclear. In this study, we examined the roles of AtDjC5 in resisting heat stress using reverse genetic analysis. After the seedlings were exposed directly to 44 °C for 90 min, AtDjC5 knockout seedlings displayed decreases in the survival rate, membrane system stability, and cell vitality compared to WT seedlings, indicating that AtDjC5 is involved in plant basal thermotolerance. The AtDjC5 knockout seedlings pre-exposed to 37 °C for 30 min exhibited decreases in the survival rate and total chlorophyll contents and increased cell death when they were subsequently exposed to 45 °C compared to the WT seedlings, indicating that AtDjC5 plays an important role in plant acquired thermotolerance. AtDjC5 was found to localize to the endoplasmic reticulum. The expression of the AtDjC5 gene was induced by heat and TM (an ER stress inducer) treatment. Furthermore, we found that the knockout of AtDjC5 inhibited ER stress-induced autophagy and the expression of ER stress-related genes. Taken together, these results suggest that AtDjC5 facilitates thermotolerance, likely by aiding in the ER stress response.

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Section: Discussionmentioning

confidence: 99%

The Arabidopsis J-Protein AtDjC5 Facilitates Thermotolerance Likely by Aiding in the ER Stress Response

Shen

Wang

Shang

et al. 2022

IJMS

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“…Pam16 and Pam18 are co-chaperones crucial for protein import into mitochondria. Plants contain multiple copies of Pam16 and Pam18 and whilst several studies have shown that Pam16 and Pam18 are targeted to mitochondria, none of these determined the localization of Pam18-1 (Tamadaddi et al, 2021). Furthermore, studies have shown that orthologues of PAM interacting partner proteins, Tim15 and Mge1, are localized to the mitochondria and plastids (Van Aken et al, 2009;Kluth et al, 2012;Langner et al, 2014).…”

Section: Discussionmentioning

confidence: 99%

“…A T-DNA insertion line for Pam16-2 was also characterized, which did not display any observable phenotype, and the double knock-out line muse5-1::pam16-2 was embryonically lethal suggesting functional overlap (Huang et al, 2013). Localization using biolistic transformation of GFP tagged Pam16-1 and Pam16-2 into onion epidermal cells identified both proteins to be targeted to mitochondria (Huang et al, 2013;Tamadaddi et al, 2021). GFP tagged constructs of Pam18-2 and Pam18-2 also identified both proteins to be targeted to the mitochondria in root cells of stable GFP fusion lines, whilst no GFP fluorescence targeting could be observed for Pam18-1 (Tamadaddi et al, 2021).…”

Section: Introductionmentioning

confidence: 99%

“…Localization using biolistic transformation of GFP tagged Pam16-1 and Pam16-2 into onion epidermal cells identified both proteins to be targeted to mitochondria (Huang et al, 2013;Tamadaddi et al, 2021). GFP tagged constructs of Pam18-2 and Pam18-2 also identified both proteins to be targeted to the mitochondria in root cells of stable GFP fusion lines, whilst no GFP fluorescence targeting could be observed for Pam18-1 (Tamadaddi et al, 2021). Three genes encode for Tim15, Tim15-2 (also known as ZR3) shown to be localized to the mitochondria, is able to functionally complement a Tim15 yeast deletion strain (Kluth et al, 2012).…”

Section: Introductionmentioning

confidence: 99%

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Presequence translocase-associated motor subunits of the mitochondrial protein import apparatus are dual-targeted to mitochondria and plastids

2022

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The import and assembly of most of the mitochondrial proteome is regulated by protein translocases located within the mitochondrial membranes. The Presequence Translocase-Associated Motor (PAM) complex powers the translocation of proteins across the inner membrane and consists of Hsp70, the J-domain containing co-chaperones, Pam16 and Pam18, and their associated proteins Tim15 and Mge1. In Arabidopsis, multiple orthologues of Pam16, Pam18, Tim15 and Mge1 have been identified and a mitochondrial localization has been confirmed for most. As the localization of Pam18-1 has yet to be determined and a plastid localization has been observed for homologues of Tim15 and Mge1, we carried out a comprehensive targeting analysis of all PAM complex orthologues using multiple in vitro and in vivo methods. We found that, Pam16 was exclusively targeted to the mitochondria, but Pam18 orthologues could be targeted to both the mitochondria and plastids, as observed for the PAM complex interacting partner proteins Tim15 and Mge1.

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“…In a similar line, Magmas ortholog, black-pearl inhibition in Drosophila melanogaster resulted in increased ROS and decreased cell proliferation ( 46 ). Recently, in Arabidopsis thaliana , two paralogs of Pam16 were identified, namely, AtPAM16 and AtPAM16L, that are required for the mitochondrial import and plant immunity ( 47 , 48 ). Hence, having the additional paralogs with evolved secondary roles raises an intriguing question about regulating Magmas levels in the mammalian system and its possible existence in multiple forms with different secondary moonlighting functions in pathological conditions.…”

mentioning

confidence: 99%

Multiple variants of the human presequence translocase motor subunit Magmas govern the mitochondrial import

Waingankar

D’Silva

2021

Journal of Biological Chemistry

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

Cited by 10 publications

References 60 publications

The Arabidopsis J-Protein AtDjC5 Facilitates Thermotolerance Likely by Aiding in the ER Stress Response

The Arabidopsis J-Protein AtDjC5 Facilitates Thermotolerance Likely by Aiding in the ER Stress Response

Presequence translocase-associated motor subunits of the mitochondrial protein import apparatus are dual-targeted to mitochondria and plastids

Multiple variants of the human presequence translocase motor subunit Magmas govern the mitochondrial import

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