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Title: Evolution of a plant-specific copper chaperone family for chloroplast copper homeostasis

Metallochaperones traffic copper (Cu +) from its point of entry at the plasma membrane to its destination. In plants, one destination is the chloroplast, which houses plastocyanin, a Cu-dependent electron transfer protein involved in photosynthesis. In this paper, we present a previously unidentified Cu + chaperone that evolved early in the plant lineage by an alternative-splicing event of the pre-mRNA encoding the chloroplast P-type ATPase in Arabidopsis 1 (PAA1). In several land plants, recent duplication events created a separate chaperone-encoding gene coincident with loss of alternative splicing. The plant-specific Cu + chaperone delivers Cu + with specificity for PAA1, which is flipped in the envelope relative to prototypical bacterial ATPases, compatible with a role in Cu + import into the stroma and consistent with the canonical catalytic mechanism of these enzymes. The ubiquity of the chaperone suggests conservation of this Cu +-delivery mechanism and provides a unique snapshot into the evolution of a Cu + distribution pathway. Finally, we also provide evidence for an interaction between PAA2, the Cu +-ATPase in thylakoids, and the Cu +-chaperone for Cu/Zn superoxide dismutase (CCS), uncovering a Cu + network that has evolved to fine-tune Cu + distribution.
Authors:
 [1] ;  [2] ;  [1] ;  [2] ;  [3]
  1. Univ. of California, Los Angeles, CA (United States). Dept. of Chemistry and Biochemistry
  2. Worcester Polytechnic Inst., MA (United States). Dept. of Chemistry and Biochemistry
  3. Univ. of California, Los Angeles, CA (United States). Dept. of Chemistry and Biochemistry. Inst. of Genomics and Proteomics
Publication Date:
Grant/Contract Number:
FC02-02ER63421; GM42143; MCB-0743901; GM100753
Type:
Accepted Manuscript
Journal Name:
Proceedings of the National Academy of Sciences of the United States of America
Additional Journal Information:
Journal Volume: 111; Journal Issue: 50; Journal ID: ISSN 0027-8424
Publisher:
National Academy of Sciences, Washington, DC (United States)
Research Org:
Univ. of California, Los Angeles, CA (United States)
Sponsoring Org:
USDOE Office of Science (SC), Biological and Environmental Research (BER) (SC-23); National Inst. of Health (NIH) (United States); National Science Foundation (NSF)
Contributing Orgs:
Worcester Polytechnic Inst., MA (United States)
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; Cu-transfer; inner envelope; metal transporter; Arabidopsis thaliana; Atx1
OSTI Identifier:
1348351

Blaby-Haas, Crysten E., Padilla-Benavides, Teresita, Stübe, Roland, Argüello, José M., and Merchant, Sabeeha S.. Evolution of a plant-specific copper chaperone family for chloroplast copper homeostasis. United States: N. p., Web. doi:10.1073/pnas.1421545111.
Blaby-Haas, Crysten E., Padilla-Benavides, Teresita, Stübe, Roland, Argüello, José M., & Merchant, Sabeeha S.. Evolution of a plant-specific copper chaperone family for chloroplast copper homeostasis. United States. doi:10.1073/pnas.1421545111.
Blaby-Haas, Crysten E., Padilla-Benavides, Teresita, Stübe, Roland, Argüello, José M., and Merchant, Sabeeha S.. 2014. "Evolution of a plant-specific copper chaperone family for chloroplast copper homeostasis". United States. doi:10.1073/pnas.1421545111. https://www.osti.gov/servlets/purl/1348351.
@article{osti_1348351,
title = {Evolution of a plant-specific copper chaperone family for chloroplast copper homeostasis},
author = {Blaby-Haas, Crysten E. and Padilla-Benavides, Teresita and Stübe, Roland and Argüello, José M. and Merchant, Sabeeha S.},
abstractNote = {Metallochaperones traffic copper (Cu+) from its point of entry at the plasma membrane to its destination. In plants, one destination is the chloroplast, which houses plastocyanin, a Cu-dependent electron transfer protein involved in photosynthesis. In this paper, we present a previously unidentified Cu+ chaperone that evolved early in the plant lineage by an alternative-splicing event of the pre-mRNA encoding the chloroplast P-type ATPase in Arabidopsis 1 (PAA1). In several land plants, recent duplication events created a separate chaperone-encoding gene coincident with loss of alternative splicing. The plant-specific Cu+ chaperone delivers Cu+ with specificity for PAA1, which is flipped in the envelope relative to prototypical bacterial ATPases, compatible with a role in Cu+ import into the stroma and consistent with the canonical catalytic mechanism of these enzymes. The ubiquity of the chaperone suggests conservation of this Cu+-delivery mechanism and provides a unique snapshot into the evolution of a Cu+ distribution pathway. Finally, we also provide evidence for an interaction between PAA2, the Cu+-ATPase in thylakoids, and the Cu+-chaperone for Cu/Zn superoxide dismutase (CCS), uncovering a Cu+ network that has evolved to fine-tune Cu+ distribution.},
doi = {10.1073/pnas.1421545111},
journal = {Proceedings of the National Academy of Sciences of the United States of America},
number = 50,
volume = 111,
place = {United States},
year = {2014},
month = {12}
}