Abstract:
:We have isolated the plasma membrane H+-ATPase in a phosphorylated form from spinach (Spinacia oleracea L.) leaf tissue incubated with fusicoccin, a fungal toxin that induces irreversible binding of 14-3-3 protein to the C terminus of the H+-ATPase, thus activating H+ pumping. We have identified threonine-948, the second residue from the C-terminal end of the H+-ATPase, as the phosphorylated amino acid. Turnover of the phosphate group of phosphothreonine-948 was inhibited by 14-3-3 binding, suggesting that this residue may form part of a binding motif for 14-3-3. This is the first identification to our knowledge of an in vivo phosphorylation site in the plant plasma membrane H+-ATPase.
journal_name
Plant Physioljournal_title
Plant physiologyauthors
Olsson A,Svennelid F,Ek B,Sommarin M,Larsson Cdoi
10.1104/pp.118.2.551subject
Has Abstractpub_date
1998-10-01 00:00:00pages
551-5issue
2eissn
0032-0889issn
1532-2548journal_volume
118pub_type
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