Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Evolutionary relationships among eubacterial groups as inferred from GroEL (chaperonin) sequence comparisons

A M Viale1, A K Arakaki, F C Soncini

  • 1Departmento de Microbiología, Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario, Argentina.

International Journal of Systematic Bacteriology
|July 1, 1994
PubMed
Summary

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

A sensitive whole-cell biosensor for the simultaneous detection of a broad-spectrum of toxic heavy metal ions.

Chemical communications (Cambridge, England)·2015
Same author

Emergence of Pseudomonas aeruginosa strains producing metallo-beta-lactamases of the IMP-15 and VIM-2 types in Mexico.

Clinical microbiology and infection : the official publication of the European Society of Clinical Microbiology and Infectious Diseases·2009
Same author

Involvement of the flavin si-face tyrosine on the structure and function of ferredoxin-NADP+ reductases.

The Journal of biological chemistry·2001
Same author

Purification of the cytosolic chaperonin TRiC from bovine testis.

Methods in molecular biology (Clifton, N.J.)·2001
Same author

Monitoring actin folding. Purification protocols for labeled proteins and binding to DNase I-sepharose beads.

Methods in molecular biology (Clifton, N.J.)·2001
Same author

Folding assays. Assessing the native conformation of proteins.

Methods in molecular biology (Clifton, N.J.)·2001

GroEL proteins, essential molecular chaperones, offer a new way to understand bacterial evolution. Phylogenetic analysis using GroEL reveals evolutionary relationships, complementing 16S rRNA data.

Area of Science:

  • Microbiology
  • Evolutionary Biology
  • Molecular Biology

Background:

  • GroEL proteins are ubiquitous molecular chaperones found in eubacteria and eukaryotic organelles.
  • Their high conservation across species makes them suitable for phylogenetic studies.

Purpose of the Study:

  • To infer eubacterial phylogenies using the highly conserved GroEL proteins.
  • To compare GroEL-based phylogenies with those derived from 16S rRNA sequencing.
  • To investigate potentially controversial or unclear evolutionary relationships within bacterial lineages.

Main Methods:

  • Phylogenetic tree construction using distance and parsimony methods based on GroEL protein sequences.
  • Comparison of resulting evolutionary trees with established 16S rRNA-based phylogenies.

Related Experiment Videos

  • Analysis of specific relationships between bacterial groups, such as Firmicutes subgroups and cyanobacteria-chloroplasts.

    • Main Results:

    • GroEL-based phylogenetic trees showed general agreement with 16S rRNA comparisons, clustering species into recognized bacterial groups.
    • Specific evolutionary relationships were inferred, including a monophyletic origin for Firmicutes subgroups (low-G+C and high-G+C) and their link to cyanobacteria-chloroplasts.
    • These findings offered clearer definitions for some relationships previously debated in rRNA-based studies.

    Conclusions:

    • GroEL proteins serve as valuable evolutionary markers for eubacterial phylogeny.
    • GroEL analysis provides complementary and sometimes clarifying insights into bacterial evolutionary history.
    • The study highlights the utility of molecular chaperones in resolving complex phylogenetic questions.