Advanced Search
Syntax
Search...
Volcani treasures
About
Terms of use
Manage
Community:
אסיף מאגר המחקר החקלאי
Powered by ClearMash Solutions Ltd -
Protein coalitions in a core mammalian biochemical network linked by rapidly evolving proteins
Year:
2011
Source of publication :
BMC Evolutionary Biology
Authors :
Freilich, Shiri
;
.
Volume :
11
Co-Authors:
Ainali, C., Department of Informatics, School of Natural and Mathematical Sciences, King's College London, Strand, London WC2R 2LS, United Kingdom
Simon, M., Bioinformatics Group, MRC Harwell, Harwell Science and Innovation Campus, Oxfordshire OX11 0RD, United Kingdom
Freilich, S., Blavatnik School of Computer Sciences, Sackler School of Medicine, Tel Aviv University, Ramat Aviv 69978, Israel
Espinosa, O., Bioinformatics Group, MRC Harwell, Harwell Science and Innovation Campus, Oxfordshire OX11 0RD, United Kingdom, Department of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, United Kingdom, Institute of Cancer Research, Chester Beattie Laboratories, London SW3 6JB, United Kingdom
Hazelwood, L., Bioinformatics Group, MRC Harwell, Harwell Science and Innovation Campus, Oxfordshire OX11 0RD, United Kingdom
Tsoka, S., Department of Informatics, School of Natural and Mathematical Sciences, King's College London, Strand, London WC2R 2LS, United Kingdom
Ouzounis, C.A., Department of Informatics, School of Natural and Mathematical Sciences, King's College London, Strand, London WC2R 2LS, United Kingdom, Computational Genomics Unit, Institute of Agrobiotechnology, Centre for Research and Technology Hellas (CERTH), GR-57001 Thessalonica, Greece
Hancock, J.M., Bioinformatics Group, MRC Harwell, Harwell Science and Innovation Campus, Oxfordshire OX11 0RD, United Kingdom
Facilitators :
From page:
To page:
(
Total pages:
1
)
Abstract:
Background: Cellular ATP levels are generated by glucose-stimulated mitochondrial metabolism and determine metabolic responses, such as glucose-stimulated insulin secretion (GSIS) from the β-cells of pancreatic islets. We describe an analysis of the evolutionary processes affecting the core enzymes involved in glucose-stimulated insulin secretion in mammals. The proteins involved in this system belong to ancient enzymatic pathways: glycolysis, the TCA cycle and oxidative phosphorylation. Results: We identify two sets of proteins, or protein coalitions, in this group of 77 enzymes with distinct evolutionary patterns. Members of the glycolysis, TCA cycle, metabolite transport, pyruvate and NADH shuttles have low rates of protein sequence evolution, as inferred from a human-mouse comparison, and relatively high rates of evolutionary gene duplication. Respiratory chain and glutathione pathway proteins evolve faster, exhibiting lower rates of gene duplication. A small number of proteins in the system evolve significantly faster than co-pathway members and may serve as rapidly evolving adapters, linking groups of co-evolving genes. Conclusions: Our results provide insights into the evolution of the involved proteins. We find evidence for two coalitions of proteins and the role of co-adaptation in protein evolution is identified and could be used in future research within a functional context. © 2011 Ainali et al; licensee BioMed Central Ltd.
Note:
Related Files :
Animal
Animals
Biochemistry
Genetics
metabolism
mice
proteins
Show More
Related Content
More details
DOI :
10.1186/1471-2148-11-142
Article number:
142
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
29036
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:43
Scientific Publication
Protein coalitions in a core mammalian biochemical network linked by rapidly evolving proteins
11
Ainali, C., Department of Informatics, School of Natural and Mathematical Sciences, King's College London, Strand, London WC2R 2LS, United Kingdom
Simon, M., Bioinformatics Group, MRC Harwell, Harwell Science and Innovation Campus, Oxfordshire OX11 0RD, United Kingdom
Freilich, S., Blavatnik School of Computer Sciences, Sackler School of Medicine, Tel Aviv University, Ramat Aviv 69978, Israel
Espinosa, O., Bioinformatics Group, MRC Harwell, Harwell Science and Innovation Campus, Oxfordshire OX11 0RD, United Kingdom, Department of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, United Kingdom, Institute of Cancer Research, Chester Beattie Laboratories, London SW3 6JB, United Kingdom
Hazelwood, L., Bioinformatics Group, MRC Harwell, Harwell Science and Innovation Campus, Oxfordshire OX11 0RD, United Kingdom
Tsoka, S., Department of Informatics, School of Natural and Mathematical Sciences, King's College London, Strand, London WC2R 2LS, United Kingdom
Ouzounis, C.A., Department of Informatics, School of Natural and Mathematical Sciences, King's College London, Strand, London WC2R 2LS, United Kingdom, Computational Genomics Unit, Institute of Agrobiotechnology, Centre for Research and Technology Hellas (CERTH), GR-57001 Thessalonica, Greece
Hancock, J.M., Bioinformatics Group, MRC Harwell, Harwell Science and Innovation Campus, Oxfordshire OX11 0RD, United Kingdom
Protein coalitions in a core mammalian biochemical network linked by rapidly evolving proteins
Background: Cellular ATP levels are generated by glucose-stimulated mitochondrial metabolism and determine metabolic responses, such as glucose-stimulated insulin secretion (GSIS) from the β-cells of pancreatic islets. We describe an analysis of the evolutionary processes affecting the core enzymes involved in glucose-stimulated insulin secretion in mammals. The proteins involved in this system belong to ancient enzymatic pathways: glycolysis, the TCA cycle and oxidative phosphorylation. Results: We identify two sets of proteins, or protein coalitions, in this group of 77 enzymes with distinct evolutionary patterns. Members of the glycolysis, TCA cycle, metabolite transport, pyruvate and NADH shuttles have low rates of protein sequence evolution, as inferred from a human-mouse comparison, and relatively high rates of evolutionary gene duplication. Respiratory chain and glutathione pathway proteins evolve faster, exhibiting lower rates of gene duplication. A small number of proteins in the system evolve significantly faster than co-pathway members and may serve as rapidly evolving adapters, linking groups of co-evolving genes. Conclusions: Our results provide insights into the evolution of the involved proteins. We find evidence for two coalitions of proteins and the role of co-adaptation in protein evolution is identified and could be used in future research within a functional context. © 2011 Ainali et al; licensee BioMed Central Ltd.
Scientific Publication
נגישות
menu      
You may also be interested in