Maize cap1 encodes a novel SERA-type calcium-ATPase with a calmodulin- binding domain

Chalivendra C. Subbaiah, Martin M. Sachs

Research output: Contribution to journalArticlepeer-review

Abstract

A cDNA (CAP1) isolated from maize roots shares sequence identity with genes encoding P-type Ca2+-ATPases and restores the growth phenotype of yeast mutants defective in Ca2+-pumps. CAP1 was transcribed and translated in the yeast mutant. Furthermore, the membrane-integrated product formed a Ca2+-dependent phosphorylated intermediate and supported Ca2+ transport. Although CAP1 shares greater sequence identity with mammalian 'endoplasmic reticulum-type' Ca2+-pumps, it differs from these genes by having features of calmodulin (CaM)-regulated Ca2+-pumps. CAP1 from yeast microsomes bound CaM, and the CAP1-dependent Ca2+ transport in yeast was stimulated by CaM. Peptides from the C terminus of CAP1 bound CaM. Anti-CAP1 antibodies specifically recognized a maize microsomal polypeptide that also bound CaM. A similar polypeptide also formed a Ca2+-dependent phosphoenzyme. Our results suggest that cap1 encodes a novel form of CaM-regulated Ca2+-ATPase in maize. CAP1 appears to be encoded by one or two genes in maize. CAP1 RNA is induced only during early anoxia, indicating that the Ca2+-pump may play an important role in O2-deprived maize cells.

Original languageEnglish (US)
Pages (from-to)21678-21687
Number of pages10
JournalJournal of Biological Chemistry
Volume275
Issue number28
DOIs
StatePublished - Jul 14 2000

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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