The chaperone connection to the origins of the eukaryotic organelles
- 21 March 1994
- journal article
- Published by Wiley in FEBS Letters
- Vol. 341 (2-3), 146-151
- https://doi.org/10.1016/0014-5793(94)80446-x
Abstract
The heat-shock 60 proteins (Hsp60) constitute a subset of molecular chaperones essential for the survival of the cell, present in eubacteria as well as in eukaryotic organelles. Here, we have employed these highly conserved proteins for the inferences of the origins of the organelles. Hsp60s present in mitochondria from different eukaryotic lineages formed a clade, which showed the closest relationship to that of the Ehrlichia/Rickettsia cluster among the α-Proteobacteria. This, in addition to phenotypic characteristics, suggests that these obligate intracellular parasites and the lineage that generated the mitochondrion shared last common ancestry. In turn, Hsp60s present in chloroplasts from plants and a red alga, respectively, clustered specifically with those of the cyanobacteria, suggesting that all plastids derive exclusively from this eubacterial lineage.Keywords
This publication has 34 references indexed in Scilit:
- Chaperonin duetNature, 1993
- A genetic rainbow of plastidsNature, 1993
- Chaperones: Helpers Along the Pathways to Protein FoldingScience, 1993
- A High-Resolution Gene Map of the Chloroplast Genome of the Red Alga Porphyra purpurea.Plant Cell, 1993
- Plastid originsTrends in Ecology & Evolution, 1992
- The sequence of the gene encoding elongation factor Tu from Chlamydia trachomatis compared with those of other organismsGene, 1992
- Phylogenetic relationships among the agent of bacillary angiomatosis, Bartonella bacilliformis, and other alpha-proteobacteriaMolecular Microbiology, 1992
- Molecular evidence for the origin of plastids from a cyanobacterium-like ancestorJournal of Molecular Evolution, 1991
- Basic local alignment search toolJournal of Molecular Biology, 1990
- PHYLOGENIES FROM MOLECULAR SEQUENCES: INFERENCE AND RELIABILITYAnnual Review of Genetics, 1988