Two subunits of the F0F1-ATPase are phosphorylated in the inner mitochondrial membrane
(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
- Struglics, André LU ; Fredlund, Kenneth M. ; Møller, Ian M. and Allen, John F. LU
- organization
- publishing date
- 1998-02-24
- 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
- pmid:9500982
- 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
- 2024-01-04 14:27:29
@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}}, }