In vitro complex formation between the octamer of mitochondrial creatine kinase and porin
Brdiczka, Dieter ; Kaldis, Philipp LU
and Wallimann, Theo
(1994)
In Journal of Biological Chemistry
269(44).
p.27640-27644
- Abstract
An interaction of mitochondrial creatine kinase with purified outer mitochondrial porin (voltage-dependent anion channel) was shown by co- sedimentation assays as well as by gel permeation chromatography. Porin formed high M(r) complexes with wild-type mitochondrial creatine kinase as well as with an N-terminal deletion mutant, lacking the first five N-terminal amino acids. The complexes were identified by creatine kinase activity in parallel with immunoblotting using specific antibodies against the two proteins. In addition, porin induced octamerization of the N-terminal creatine kinase mutant, which under the same conditions without porin, did not polymerize but remained more than 90% dimeric. Furthermore, binding of mitochondrial... (More)
An interaction of mitochondrial creatine kinase with purified outer mitochondrial porin (voltage-dependent anion channel) was shown by co- sedimentation assays as well as by gel permeation chromatography. Porin formed high M(r) complexes with wild-type mitochondrial creatine kinase as well as with an N-terminal deletion mutant, lacking the first five N-terminal amino acids. The complexes were identified by creatine kinase activity in parallel with immunoblotting using specific antibodies against the two proteins. In addition, porin induced octamerization of the N-terminal creatine kinase mutant, which under the same conditions without porin, did not polymerize but remained more than 90% dimeric. Furthermore, binding of mitochondrial creatine kinase to porin affected the conductance of porin when reconstituted in 'black membranes.' At 10 mV the pore in the complex adopted a low conductance (1.5-2 nanosiemens) state, compared to the high conductance state (3-4 nanosiemens) of the free incorporated pores. The former state of the pore is known to be cationically selective. Thus, besides a specific structural interaction, a defined physiological function is assumed of the mitochondrial creatine kinase-porin complexes that are discussed here.
(Less)
- author
- Brdiczka, Dieter
; Kaldis, Philipp
LU
and Wallimann, Theo
- publishing date
- 1994-11-04
- type
- Contribution to journal
- publication status
- published
- in
- Journal of Biological Chemistry
- volume
- 269
- issue
- 44
- pages
- 5 pages
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- pmid:7525559
- scopus:0028034636
- ISSN
- 0021-9258
- language
- English
- LU publication?
- no
- id
- b5bd3e96-9a2f-4ab5-83a6-444ee9ba85ce
- alternative location
- http://www.jbc.org/content/269/44/27640.full.pdf
- date added to LUP
- 2019-09-18 14:38:48
- date last changed
- 2024-01-01 20:51:53
@article{b5bd3e96-9a2f-4ab5-83a6-444ee9ba85ce,
abstract = {{<p>An interaction of mitochondrial creatine kinase with purified outer mitochondrial porin (voltage-dependent anion channel) was shown by co- sedimentation assays as well as by gel permeation chromatography. Porin formed high M(r) complexes with wild-type mitochondrial creatine kinase as well as with an N-terminal deletion mutant, lacking the first five N-terminal amino acids. The complexes were identified by creatine kinase activity in parallel with immunoblotting using specific antibodies against the two proteins. In addition, porin induced octamerization of the N-terminal creatine kinase mutant, which under the same conditions without porin, did not polymerize but remained more than 90% dimeric. Furthermore, binding of mitochondrial creatine kinase to porin affected the conductance of porin when reconstituted in 'black membranes.' At 10 mV the pore in the complex adopted a low conductance (1.5-2 nanosiemens) state, compared to the high conductance state (3-4 nanosiemens) of the free incorporated pores. The former state of the pore is known to be cationically selective. Thus, besides a specific structural interaction, a defined physiological function is assumed of the mitochondrial creatine kinase-porin complexes that are discussed here.</p>}},
author = {{Brdiczka, Dieter and Kaldis, Philipp and Wallimann, Theo}},
issn = {{0021-9258}},
language = {{eng}},
month = {{11}},
number = {{44}},
pages = {{27640--27644}},
publisher = {{American Society for Biochemistry and Molecular Biology}},
series = {{Journal of Biological Chemistry}},
title = {{In vitro complex formation between the octamer of mitochondrial creatine kinase and porin}},
url = {{http://www.jbc.org/content/269/44/27640.full.pdf}},
volume = {{269}},
year = {{1994}},
}