Senescence-induced, thylakoid-bound diisopropylfluorophosphate-binding protein in spinach : induction pattern, localization, and some properties.

Abstract:

:Changes in diisopropylfluorophosphate (DFP)-binding proteins during development and senescence of spinach (Spinacia oleracea) leaves were followed using [(3)H]DFP and sodium dodecylsulfate-polyacrylamide gel electrophoresis-fluorography. Experiments using a series of aging stages of leaves attached to plants and ones with detached leaves stored in the dark both showed that a protein of 38 kilodaltons was the only major DFP-binding protein in the membrane fraction and that its DFP-binding increased markedly as senescence proceeded, corresponding with the degradation of leaf protein. DFP binding to the 38-kilodalton protein was not affected by membrane solubilization with Triton X-100, and gradually decreased upon preservation of the membranes. The DFP binding was inhibited completely by phenylmethane-sulfonyl fluoride and slightly by p-chloromercuribenzoic acid, suggesting a serine protease-like character of the protein and a possible contribution of SH residues to the binding. Both differential and Percoll-gradient centrifugation indicated that the 38-kilodalton protein was localized in thylakoid membranes. The sedimentation behavior of the detergent-solubilized protein indicated that it belongs to a complex different from photosystem I, photosystem II, or coupling factor 1 of the ATP-synthesizing complex.

journal_name

Plant Physiol

journal_title

Plant physiology

authors

Kawasaki S,Takeuchi J

doi

10.1104/pp.90.1.338

subject

Has Abstract

pub_date

1989-05-01 00:00:00

pages

338-44

issue

1

eissn

0032-0889

issn

1532-2548

journal_volume

90

pub_type

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