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The distribution of charged amino acids in mitochondrial inner-membrane proteins suggests different modes of membrane integration for nuclearly and mitochondrially encoded proteins.
- Source :
- European Journal of Biochemistry; 5/1/92, Vol. 205 Issue 3, p1207-1215, 9p, 1 Diagram, 4 Charts, 2 Graphs
- Publication Year :
- 1992
-
Abstract
- We have analyzed the amino acid distribution in seven nuclearly encoded and five mitochondrially encoded inner membrane proteins with experimentally well characterized topologies. The mitochondrially encoded proteins conform to the ‘positive inside’ rule, i.e. they have many more positively charged residues in their non-translocated as compared to translocated domains. However, most of the nuclearly encoded proteins do not show such a bias but instead have a surprisingly skewed distribution of Glu residues with an almost ten times higher frequency in the intermembrane space than in the matrix domains. These findings suggest that some, but possibly not all, nuclearly encoded inner membrane proteins may insert into the membrane by a mechanism that does not depend on the distribution of positively charged amino acids. [ABSTRACT FROM AUTHOR]
- Subjects :
- AMINO acids
MEMBRANE proteins
ORGANIC acids
MITOCHONDRIA
PROTEINS
ORGANIC compounds
Subjects
Details
- Language :
- English
- ISSN :
- 00142956
- Volume :
- 205
- Issue :
- 3
- Database :
- Complementary Index
- Journal :
- European Journal of Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 13684161
- Full Text :
- https://doi.org/10.1111/j.1432-1033.1992.tb16892.x