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Two subunits of the F0F1-ATPase are phosphorylated in the inner mitochondrial membrane

Struglics, André LU ; Fredlund, Kenneth M. ; Møller, Ian M. and Allen, John F. LU (1998) In Biochemical and Biophysical Research Communications 243(3). p.664-668
Abstract

Inside-out submitochondrial particles from potato tuber mitochondria were incubated with [γ-32P]ATP. More than 16 phosphorylated polypeptides were detected by autoradiography on an SDS-gel. Two phosphoproteins, migrating at 22 and 28 kDa, were excised from the SDS-gel, electroeluted, and purified further by anion chromatography. The phosphoproteins were N-terminally sequenced. Over the regions sequenced, the 22 and 28 kDa phosphoproteins had 100% sequence identity with potato proteins identified as the δ'-subunit of the F1-ATPase and the b-subunit of the F0-ATPase, respectively. We suggest that phosphorylation of these proteins may control the interaction between F1 and F0 and... (More)

Inside-out submitochondrial particles from potato tuber mitochondria were incubated with [γ-32P]ATP. More than 16 phosphorylated polypeptides were detected by autoradiography on an SDS-gel. Two phosphoproteins, migrating at 22 and 28 kDa, were excised from the SDS-gel, electroeluted, and purified further by anion chromatography. The phosphoproteins were N-terminally sequenced. Over the regions sequenced, the 22 and 28 kDa phosphoproteins had 100% sequence identity with potato proteins identified as the δ'-subunit of the F1-ATPase and the b-subunit of the F0-ATPase, respectively. We suggest that phosphorylation of these proteins may control the interaction between F1 and F0 and regulate energy coupling in oxidative phosphorylation.

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author
; ; and
organization
publishing date
type
Contribution to journal
publication status
published
keywords
F(o)F-ATPase, Inner mitochondrial membrane, Mitochondria, Protein phosphorylation
in
Biochemical and Biophysical Research Communications
volume
243
issue
3
pages
664 - 668
publisher
Elsevier
external identifiers
  • pmid:9500982
  • scopus:0032562028
ISSN
0006-291X
DOI
10.1006/bbrc.1998.8151
language
English
LU publication?
yes
id
fc9a80b2-3687-4172-a897-2e308f3ddaa9
date added to LUP
2016-10-14 16:01:58
date last changed
2025-10-14 10:01:03
@article{fc9a80b2-3687-4172-a897-2e308f3ddaa9,
  abstract     = {{<p>Inside-out submitochondrial particles from potato tuber mitochondria were incubated with [γ-<sup>32</sup>P]ATP. More than 16 phosphorylated polypeptides were detected by autoradiography on an SDS-gel. Two phosphoproteins, migrating at 22 and 28 kDa, were excised from the SDS-gel, electroeluted, and purified further by anion chromatography. The phosphoproteins were N-terminally sequenced. Over the regions sequenced, the 22 and 28 kDa phosphoproteins had 100% sequence identity with potato proteins identified as the δ'-subunit of the F<sub>1</sub>-ATPase and the b-subunit of the F<sub>0</sub>-ATPase, respectively. We suggest that phosphorylation of these proteins may control the interaction between F<sub>1</sub> and F<sub>0</sub> and regulate energy coupling in oxidative phosphorylation.</p>}},
  author       = {{Struglics, André and Fredlund, Kenneth M. and Møller, Ian M. and Allen, John F.}},
  issn         = {{0006-291X}},
  keywords     = {{F(o)F-ATPase; Inner mitochondrial membrane; Mitochondria; Protein phosphorylation}},
  language     = {{eng}},
  month        = {{02}},
  number       = {{3}},
  pages        = {{664--668}},
  publisher    = {{Elsevier}},
  series       = {{Biochemical and Biophysical Research Communications}},
  title        = {{Two subunits of the F0F1-ATPase are phosphorylated in the inner mitochondrial membrane}},
  url          = {{http://dx.doi.org/10.1006/bbrc.1998.8151}},
  doi          = {{10.1006/bbrc.1998.8151}},
  volume       = {{243}},
  year         = {{1998}},
}