Evolution of a plant-specific copper chaperone family for chloroplast copper homeostasis [electronic resource]

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Ngôn ngữ: eng

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Thông tin xuất bản: Washington, D.C. : Oak Ridge, Tenn. : United States. Dept. of Energy. Office of Science ; Distributed by the Office of Scientific and Technical Information, U.S. Dept. of Energy, 2014

Mô tả vật lý: Size: p. E5480-E5487 : , digital, PDF file.

Bộ sưu tập: Metadata

ID: 261266

 Metallochaperones traffic copper (Cu<
 sup>
 +<
 /sup>
 ) 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<
 sup>
 +<
 /sup>
  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<
 sup>
 +<
 /sup>
  chaperone delivers Cu<
 sup>
 +<
 /sup>
  with specificity for PAA1, which is flipped in the envelope relative to prototypical bacterial ATPases, compatible with a role in Cu<
 sup>
 +<
 /sup>
  import into the stroma and consistent with the canonical catalytic mechanism of these enzymes. The ubiquity of the chaperone suggests conservation of this Cu<
 sup>
 +<
 /sup>
 -delivery mechanism and provides a unique snapshot into the evolution of a Cu<
 sup>
 +<
 /sup>
  distribution pathway. Finally, we also provide evidence for an interaction between PAA2, the Cu<
 sup>
 +<
 /sup>
 -ATPase in thylakoids, and the Cu<
 sup>
 +<
 /sup>
 -chaperone for Cu/Zn superoxide dismutase (CCS), uncovering a Cu<
 sup>
 +<
 /sup>
  network that has evolved to fine-tune Cu<
 sup>
 +<
 /sup>
  distribution.
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