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231224s2015 xx |||||o 00| ||eng c |
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|a 10.1111/nph.13093
|2 doi
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|a pubmed24n0807.xml
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|a (DE-627)NLM242289533
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|a (NLM)25262970
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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1 |
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|a Tapken, Wiebke
|e verfasserin
|4 aut
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|a The Clp protease system is required for copper ion-dependent turnover of the PAA2/HMA8 copper transporter in chloroplasts
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|c 2015
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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|a Date Completed 31.08.2015
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|a Date Revised 30.09.2020
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a © 2014 The Authors. New Phytologist © 2014 New Phytologist Trust.
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|a The distribution of essential metal ions over subcellular compartments for use as cofactors requires control of membrane transporters. PAA2/HMA8 is a copper-transporting P1B -type ATPase in the thylakoid membrane, required for the maturation of plastocyanin. When copper is highly available to the plant this transporter is degraded, which implies the action of a protease. In order to identify the proteolytic machinery responsible for PAA2/HMA8 turnover in Arabidopsis, mutant lines defective in five different chloroplast protease systems were analyzed. Plants defective in the chloroplast caseinolytic protease (Clp) system were specifically impaired in PAA2/HMA8 protein turnover on media containing elevated copper concentrations. However, the abundance of a core Clp component was not directly affected by copper. Furthermore, the expression and activity of both cytosolic and chloroplast-localized superoxide dismutases (SODs), which are known to be dependent on copper, were not altered in the clp mutants, indicating that the loss of PAA2/HMA8 turnover in these lines was not caused by a lack of stromal copper. The results suggest that copper excess in the stroma triggers selection of the thylakoid-localized PAA2 transporter for degradation by the Clp protease, but not several other chloroplast proteases, and support a novel role for this proteolytic system in cellular copper homeostasis
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|a Journal Article
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|a Research Support, U.S. Gov't, Non-P.H.S.
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|a P1B-type ATPase
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|a caseinolytic protease (Clp)
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|a chloroplast
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|a copper (Cu) homeostasis
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|a copper transport
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|a proteolysis
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|a regulated protein turnover
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|a Arabidopsis Proteins
|2 NLM
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|a Cation Transport Proteins
|2 NLM
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|a Membrane Transport Proteins
|2 NLM
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|a Copper
|2 NLM
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| 650 |
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|a 789U1901C5
|2 NLM
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| 650 |
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|a Superoxide Dismutase
|2 NLM
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| 650 |
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|a EC 1.15.1.1
|2 NLM
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|a Endopeptidase Clp
|2 NLM
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| 650 |
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|a EC 3.4.21.92
|2 NLM
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|a Adenosine Triphosphatases
|2 NLM
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|a EC 3.6.1.-
|2 NLM
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|a Chloroplast Proton-Translocating ATPases
|2 NLM
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|a EC 3.6.3.-
|2 NLM
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|a PAA2 protein, Arabidopsis
|2 NLM
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| 650 |
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|a EC 3.6.3.-
|2 NLM
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| 650 |
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|a Copper-Transporting ATPases
|2 NLM
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| 650 |
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|a EC 7.2.2.8
|2 NLM
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| 700 |
1 |
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|a Kim, Jitae
|e verfasserin
|4 aut
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|a Nishimura, Kenji
|e verfasserin
|4 aut
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| 700 |
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|a van Wijk, Klaas J
|e verfasserin
|4 aut
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| 700 |
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|a Pilon, Marinus
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t The New phytologist
|d 1979
|g 205(2015), 2 vom: 07. Jan., Seite 511-7
|w (DE-627)NLM09818248X
|x 1469-8137
|7 nnns
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| 773 |
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|g volume:205
|g year:2015
|g number:2
|g day:07
|g month:01
|g pages:511-7
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|u http://dx.doi.org/10.1111/nph.13093
|3 Volltext
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|a AR
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|d 205
|j 2015
|e 2
|b 07
|c 01
|h 511-7
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