Plastocyanin Controls the Stabilization of the Thylakoid Cu-transporting P-type ATPase PAA2/HMA8 in Response to Low Copper in Arabidopsis

Tapken, Wiebke; Ravet, Karl; Pilon, Marinus

doi:10.1074/jbc.m111.318204

Cited by 46 publications

(58 citation statements)

References 35 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…AtHMA6 (or PAA1), localized in the inner chloroplast envelope, is responsible for the delivery of Cu to chloroplasts (Catty et al, 2011). AtHMA8 (PAA2), closely related to AtHMA6 (PAA1), is expressed in the thylakoid membrane and supplies Cu to plastocyanin (Tapken et al, 2012). AtHMA1 and HvHMA1, present in the chloroplast envelope, are broad-specificity exporters of metals from chloroplasts and may play a specialized role in Cu mobilization (Mikkelsen et al, 2012).…”

Section: Copper Uptake By Plantsmentioning

confidence: 99%

Influence of Soil Chemistry and Plant Physiology in the Phytoremediation of Cu, Mn, and Zn

Pinto

Aguiar

Ferreira

2014

Critical Reviews in Plant Sciences

View full text Add to dashboard Cite

Section: Copper Uptake By Plantsmentioning

confidence: 99%

Influence of Soil Chemistry and Plant Physiology in the Phytoremediation of Cu, Mn, and Zn

Pinto

Aguiar

Ferreira

2014

Critical Reviews in Plant Sciences

View full text Add to dashboard Cite

“…PAA2/HMA8 abundance is down-regulated in response to high copper concentrations (Tapken et al, 2012). This copper-induced down-regulation involves proteolysis by the stromal Clp system rather than thylakoid-located FtsH protease (Tapken et al, 2015).…”

Section: Regulation Of Metal Homeostasismentioning

confidence: 99%

“…Another copper transporter, PAA1/HMA6, is present in the inner envelope membrane (Shikanai et al, 2003). Its accumulation is unaffected by high-copper conditions (Tapken et al, 2012). It is noteworthy that some of the ClpS1 targets isolated through affinity purification are metal-binding or metal-related proteins (Nishimura et al, 2013).…”

Section: Regulation Of Metal Homeostasismentioning

confidence: 99%

Chloroplast Proteases: Updates on Proteolysis within and across Suborganellar Compartments

2016

View full text Add to dashboard Cite

ORCID IDs: 0000-0003-1718-9121 (Y.K.); 0000-0001-9747-5042 (W.S.).Chloroplasts originated from the endosymbiosis of ancestral cyanobacteria and maintain transcription and translation machineries for around 100 proteins. Most endosymbiont genes, however, have been transferred to the host nucleus, and the majority of the chloroplast proteome is composed of nucleus-encoded proteins that are biosynthesized in the cytosol and then imported into chloroplasts. How chloroplasts and the nucleus communicate to control the plastid proteome remains an important question. Protein-degrading machineries play key roles in chloroplast proteome biogenesis, remodeling, and maintenance. Research in the past few decades has revealed more than 20 chloroplast proteases, which are localized to specific suborganellar locations. In particular, two energy-dependent processive proteases of bacterial origin, Clp and FtsH, are central to protein homeostasis. Processing endopeptidases such as stromal processing peptidase and thylakoidal processing peptidase are involved in the maturation of precursor proteins imported into chloroplasts by cleaving off the amino-terminal transit peptides. Presequence peptidases and organellar oligopeptidase subsequently degrade the cleaved targeting peptides. Recent findings have indicated that not only intraplastidic but also extraplastidic processive protein-degrading systems participate in the regulation and quality control of protein translocation across the envelopes. In this review, we summarize current knowledge of the major chloroplast proteases in terms of type, suborganellar localization, and diversification. We present details of these degradation processes as case studies according to suborganellar compartment (envelope, stroma, and thylakoids). Key questions and future directions in this field are discussed.Over 1 billion years of plastid evolution since the endosymbiosis of ancestral cyanobacteria (Douzery et al., 2004), chloroplast biogenesis has gained complexity, with large sets of the endosymbiont genes being transferred to host nuclear genomes. While only 100 endosymbiont genes remain in the plastid genome, with the corresponding proteins biosynthesized there, the nuclear genes have often gained complexity by duplication and diversification of the original endosymbiotic genes. This complexity raises numerous questions regarding (1) at what level gene expression is coordinately controlled, (2) what molecules coordinate the cross talk between chloroplasts and the nucleus, (3) how proteins get across membranes and become imported into chloroplasts, and (4) how the stoichiometries of nucleus-and chloroplast-encoded subunits within individual chloroplast protein complexes such as photosystems and Rubisco are strictly maintained.Given these questions, chloroplast biogenesis has remained a central subject in plant physiology for the last few decades (Jarvis and López-Juez, 2013). In our view, the aforementioned questions point to the importance of protein homeostasis and posttranslational modificat...

show abstract

“…RAN1 P-type ATPase pumps cytosolic Cu toward the secretory pathway for incorporation into Cu-proteins such as the ethylene receptor [25,26]. PAA1 ATPase, which is located in the inner chloroplast envelope, mediates Cu transport from the cytoplasm to plastid stroma, and the thylakoid-located PAA2 facilitates final Cu delivery to plastocyanin into the thylakoid lumen [17,27,28]. Therefore upon Cu scarcity, cofactor delivery to multiple nonessential or replaceable Cuconsuming enzymes is reduced to prioritize the utilization of Cu in essential Cu-dependent processes such as photosynthetic electron transport [28,29].…”

Section: Introductionmentioning

confidence: 99%

Function and Regulation of the Plant COPT Family of High-Affinity Copper Transport Proteins

Puig

2014

Advances in Botany

View full text Add to dashboard Cite

Copper (Cu) is an essential micronutrient for all eukaryotes because it participates as a redox active cofactor in multiple biological processes, including mitochondrial respiration, photosynthesis, oxidative stress protection, and iron (Fe) transport. In eukaryotic cells, Cu transport toward the cytoplasm is mediated by the conserved CTR/COPT family of high-affinity Cu transport proteins. This outlook paper reviews the contribution of our research group to the characterization of the function played by the Arabidopsis thaliana COPT1-6 family of proteins in plant Cu homeostasis. Our studies indicate that the different tissue specificity, Curegulated expression, and subcellular localization dictate COPT-specialized contribution to plant Cu transport and distribution. By characterizing lack-of-function Arabidopsis mutant lines, we conclude that COPT1 mediates root Cu acquisition, COPT6 facilitates shoot Cu distribution, and COPT5 mobilizes Cu from storage organelles. Furthermore, our work with copt2 mutant and COPToverexpressing plants has also uncovered Cu connections with Fe homeostasis and the circadian clock, respectively. Future studies on the interaction between COPT transporters and other components of the Cu homeostasis network will improve our knowledge of plant Cu acquisition, distribution, regulation, and utilization by Cu-proteins.

show abstract

Plastocyanin Controls the Stabilization of the Thylakoid Cu-transporting P-type ATPase PAA2/HMA8 in Response to Low Copper in Arabidopsis

Cited by 46 publications

References 35 publications

Influence of Soil Chemistry and Plant Physiology in the Phytoremediation of Cu, Mn, and Zn

Influence of Soil Chemistry and Plant Physiology in the Phytoremediation of Cu, Mn, and Zn

Chloroplast Proteases: Updates on Proteolysis within and across Suborganellar Compartments

Function and Regulation of the Plant COPT Family of High-Affinity Copper Transport Proteins

Contact Info

Product

Resources

About