DOI: 10.1111/j.1432-1033.1988.tb14241.x. Phosphorylation of a 51‐kDa envelope membrane polypeptide involved in protein translocation into chloroplasts

Phosphorylation of a 51‐kDa envelope membrane polypeptide involved in protein translocation into chloroplasts

10.1111/j.1432-1033.1988.tb14241.x

Crossref journal-article

Wiley

European Journal of Biochemistry (311)

Abstract

In this report we demonstrate that a 51‐kDa outer‐envelope membrane protein (P51) is involved in protein translocation into chloroplasts. Furthermore it is shown that phosphorylation of P51 is functionally related to the process of binding and/or importing precursor proteins into chloroplasts. Several lines of evidence have been obtained supporting this suggestion. First, protein import into chloroplasts was inhibited by the membrane‐impermeable agent pyridoxal 5′‐phosphate, which has been shown to react with a component of the protein‐import apparatus. Phosphorylation of envelope membrane polypeptides using [γ‐32P]ATP in the presence of pyridoxal 5′‐phosphate resulted in an increased incorporation of 32P radiolabel into a 51‐kDa membrane polypeptide (P51). A close correlation between the inhibition of protein import and the increase in the phosphorylation state of P51, both as a function of PLP concentration, was observed. Second, binding of purified precursor proteins to chloroplasts resulted in a specific increase in the phosphorylation state of P51. This effect was not exerted by the mature form of the precursor protein lacking the presequence. Third, internally generated ATP was able to compete specifically with externally added [γ‐32P]ATP for the phosphorylation of P51. Fourth, digestion of the outer‐envelope membrane with low amounts of thermolysin resulted in a loss of protein import activity, which was associated with the removal of the phosphorylation site of P51.Phosphorylation of P51 proceeds with an apparent Km (ATP) of about 5 μM, which is much lower than the ATP concentration required for the protein translocation itself. We suggest that two different ATP‐dependent processes are involved in protein translocation into chloroplasts. P51 represent presumably a regulatory component of the protein‐import apparatus or the protein receptor itself.

Bibliography

HINZ, G., & FLÃGGE, U. I. (1988). Phosphorylation of a 51âkDa envelope membrane polypeptide involved in protein translocation into chloroplasts. European Journal of Biochemistry, 175(3), 649â659. Portico.

Authors 2

Giselbert HINZ (first)
Ulf Ingo FLÜGGE (additional)

References 62 Referenced 35

Dates

Type	When
Created	20 years, 5 months ago (March 3, 2005, 9:21 p.m.)
Deposited	1 year, 8 months ago (Nov. 22, 2023, 9:46 p.m.)
Indexed	1 year, 8 months ago (Nov. 22, 2023, 10:10 p.m.)
Issued	37 years ago (Aug. 1, 1988)
Published	37 years ago (Aug. 1, 1988)
Published Online	20 years, 5 months ago (March 3, 2005)
Published Print	37 years ago (Aug. 1, 1988)

Funders 0

None

BibTeX

@article{HINZ_1988, title={Phosphorylation of a 51‐kDa envelope membrane polypeptide involved in protein translocation into chloroplasts}, volume={175}, ISSN={1432-1033}, url={http://dx.doi.org/10.1111/j.1432-1033.1988.tb14241.x}, DOI={10.1111/j.1432-1033.1988.tb14241.x}, number={3}, journal={European Journal of Biochemistry}, publisher={Wiley}, author={HINZ, Giselbert and FLÜGGE, Ulf Ingo}, year={1988}, month=aug, pages={649–659} }

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