AtTPR7 is a chaperone docking protein of the Sec translocon in <i>Arabidopsis</i>

Schweiger, Regina; Müller, Nina; Soll, Jürgen; Schwenkert, Serena

doi:10.1242/jcs.111054

Cited by 32 publications

(43 citation statements)

References 71 publications

(106 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The Agrobacterium tumefaciens strain AGL1 was transformed with the full coding sequence of AtmtTatB (At5g43680) fused to GFP in the vector pK7FWG2 (Karimi et al, 2002) and used to infiltrate 4-6 week old Nicotiana benthamiana leaves as described previously (Schweiger et al, 2012). Protoplasts were prepared as outlined in Koop et al (1996), except cell walls were digested for 90 min at 40 rpm in 1% cellulase R10 and 0.3% macerase R10 after vacuum infiltration.…”

Section: Gfp Subcellular Localizationmentioning

confidence: 99%

Plant mitochondria contain the protein translocase subunits TatB and TatC

Carrie

Weißenberger

Soll

2016

Journal of Cell Science

Self Cite

View full text Add to dashboard Cite

Twin-arginine translocation (Tat) pathways have been wellcharacterized in bacteria and chloroplasts. Genes encoding a TatC protein are found in almost all plant mitochondrial genomes but to date these have not been extensively investigated. For the first time it could be demonstrated that this mitochondrial-encoded TatC is a functional gene that is translated into a protein in the model plant Arabidopsis thaliana. A TatB-like subunit localized to the inner membrane was also identified that is nuclear-encoded and is essential for plant growth and development, indicating that plants potentially require a Tat pathway for mitochondrial biogenesis.

show abstract

Section: Gfp Subcellular Localizationmentioning

confidence: 99%

Plant mitochondria contain the protein translocase subunits TatB and TatC

Carrie

Weißenberger

Soll

2016

Journal of Cell Science

Self Cite

View full text Add to dashboard Cite

show abstract

“…15 Further analyses suggest Sec62 as additional interaction partner of AtTPR7 not only by in vitro pull down experiments but also in vivo performing a bimolecular fluorescence complementation assay (BiFC) (Fig. 2).…”

Section: Attpr7 As Part Of the Arabidopsis Sec Post-transloconmentioning

confidence: 93%

AtTPR7 as part of theArabidopsisSec post-translocon

Schweiger

Schwenkert

2013

Plant Signaling & Behavior

Self Cite

View full text Add to dashboard Cite

The secretory pathway regulates proper targeting of proteins synthesized on cytosolic ribosomes to their destined compartments through the endoplasmic reticulum (ER) and the golgi apparatus as well as via the plasma membrane to the extracellular matrix. The first step in this pathway is the translocation of the newly synthesized proteins into the ER which can occur either co-or post-translationally. 1,2During co-translational translocation elongation of the protein is arrested due to binding of the signal recognition particle (SRP) to the freshly synthesized nascent polypeptide chain appearing at the ribosome. Translation continues after binding of the SRP to the SRP receptor at the ER membrane and the polypeptide is translocated through the Sec61 channel into the ER. In the post-translational pathway proteins are first fully synthesized in the cytosol and therefore released from the ribosomes before being translocated. It was shown that predominantly small secretory proteins are translocated post-translationally into the ER in yeast and mammals. These small proteins are expected to be inefficiently recognized by the SRP at the ribosome since translation is completed only shortly after exposure of the N-terminal signal sequence.4 This post-translational transport is typically facilitated by molecular chaperones such as the heat shock protein 70 (HSP70) in the cytosol. 5 In yeast post-translational translocation requires a heptameric Sec complex at the ER membrane, consisting of a tetrameric Sec62/63p complex The secretory system in eukaryotic organisms ensures targeting of proteins to their place of function after they entered the endoplasmic reticulum either co-or post-translationally. Thereby proteins are translocated through the Sec translocon into the endoplasmic reticulum. In the Arabidopsis genome homologs for the three major components of the Sec translocon, the central pore Sec61α and the auxiliary proteins Sec62 and Sec63 are present. Phylogenetic analyses show Sec61α to be the most conserved subunit within the Sec translocon whereas Sec62 and Sec63 show less homology but contain the same functional domains among all organisms. We recently characterized a novel tetratricopeptide repeat domain containing protein, AtTPR7, as part of the Arabidopsis Sec translocon which is probably involved in chaperone assisted post-translational import. In this study we investigated the interaction of AtTPR7 with Sec62 as well as the cytosolic chaperones HSP70 and HSP90 not only in vitro but also in vivo to further strengthen the hypothesis of AtTPR7 being a chaperone docking protein of the Sec translocon for secretory preproteins in Arabidopsis.

show abstract

“…Likewise, neither the loss of the mitochondrial OM64 and ER AtTPR7 results in any visible phenotype Schweiger et al , 2012 ).…”

Section: The Molecular Framework Of the Toc Complexmentioning

confidence: 97%

“…In plants, apart from Toc64, TPR-mediated preprotein translocation has thus far been reported for the mitochondrial outer envelope protein, OM64 and recently, the endoplasmic reticulum (ER) TPR-docking protein, AtTPR7. Both proteins have been shown to interact with chaperones and preproteins Lister et al , 2007 ;Schweiger et al , 2012 ). Intriguingly, both OM64 and AtTPR7 can functionally complement yeast mitochondrial Δ tom70 and Δ sec71 , respectively, thus hinting at a potential function in post-translational protein translocation across the mitochondria and ER membrane.…”

Section: The Molecular Framework Of the Toc Complexmentioning

confidence: 99%

The gateway to chloroplast: re-defining the function of chloroplast receptor proteins

Chang¹,

Soll²,

Bölter³

2012

Biological Chemistry

Self Cite

View full text Add to dashboard Cite

: Chloroplast biogenesis often requires a tight orchestration between gene expression (both plastidial and nuclear) and translocation of ~ 3000 nuclear-encoded proteins into the organelle. Protein translocation is achieved via two multimeric import machineries at the outer (TOC) and inner (TIC) envelope of chloroplast, respectively. Three components constitute the core element of the TOC complex: a β -barrel protein translocation channel Toc75 and two receptor constituents, Toc159 and Toc34. A diverse set of distinct TOC complexes have recently been characterized and these diversified TOC complexes have evolved to coordinate the translocation of differentially expressed proteins. This review aims to describe the recent discoveries relating to the typical characteristics of these distinct TOC complexes, particularly the receptor constituents, which are the main contributors for TOC complex diversification.

show abstract

AtTPR7 is a chaperone docking protein of the Sec translocon in Arabidopsis

Cited by 32 publications

References 71 publications

Plant mitochondria contain the protein translocase subunits TatB and TatC

Plant mitochondria contain the protein translocase subunits TatB and TatC

AtTPR7 as part of theArabidopsisSec post-translocon

The gateway to chloroplast: re-defining the function of chloroplast receptor proteins

Contact Info

Product

Resources

About