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Reciprocal domain evolution within a transactivator in a restricted sequence space.

K Juarez1, H Flores, S Dávila

  • 1Instituto de Biotecnologia, Universidad Nacional Autónoma de México, AP 510-3, Cuernavaca, Morelos, 62250, Mexico.

Proceedings of the National Academy of Sciences of the United States of America
|March 15, 2000
PubMed
Summary

Protein domains coevolve, as seen in Sinorhizobium meliloti NifA (SmNifA). A defect in SmNifA's DNA-binding was compensated by an efficient activation domain, mimicking natural evolution.

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Area of Science:

  • Molecular Biology
  • Evolutionary Biology
  • Protein Science

Background:

  • Protein evolution involves domain shuffling and merging.
  • Demonstrating domain coadaptation has been challenging.
  • The Sinorhizobium meliloti NifA (SmNifA) protein provides a model for studying coevolution.

Purpose of the Study:

  • To provide evidence for the coevolution of domains within the SmNifA protein.
  • To understand how functional defects in one domain are compensated by others.
  • To explore the evolutionary pathways of NifA activity.

Main Methods:

  • Comparative analysis of SmNifA and Bradyrhizobium japonicum NifA (BjNifA).
  • Site-directed mutagenesis of BjNifA.
  • Selection experiments to identify highly active NifA variants.

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Main Results:

  • SmNifA exhibits weak enhancer interaction due to a glycine deficiency in its DNA-binding domain.
  • This interaction defect is compensated by a highly efficient, trans-activating domain.
  • Mutagenesis of BjNifA yielded variants with mutations identical to those found in SmNifA.
  • Artificial evolution recreated the natural evolutionary path of NifA.

Conclusions:

  • NifA evolution is constrained within a limited sequence space.
  • Point mutations offer restricted solutions for enhancing NifA activity.
  • The study demonstrates domain coadaptation and provides insights into protein evolution.