Advanced

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.

(Less)
Please use this url to cite or link to this publication:
author
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
  • 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
2016-11-30 16:54:37
@misc{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},
  keyword      = {F(o)F-ATPase,Inner mitochondrial membrane,Mitochondria,Protein phosphorylation},
  language     = {eng},
  month        = {02},
  number       = {3},
  pages        = {664--668},
  publisher    = {ARRAY(0x80d5fa0)},
  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},
  volume       = {243},
  year         = {1998},
}