The thermostability and specificity of ancient proteins

Lucas C Wheeler; Shion A Lim; Susan Marqusee; Michael J Harms

doi:10.1016/j.sbi.2016.05.015

The thermostability and specificity of ancient proteins

Curr Opin Struct Biol. 2016 Jun:38:37-43. doi: 10.1016/j.sbi.2016.05.015. Epub 2016 Jun 9.

Authors

Lucas C Wheeler¹, Shion A Lim², Susan Marqusee³, Michael J Harms⁴

Affiliations

¹ Department of Chemistry and Biochemistry, University of Oregon, Eugene, OR, United States; Institute of Molecular Biology, University of Oregon, Eugene, OR, United States.
² Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA, United States; Institute for Quantitative Biosciences (QB3), University of California, Berkeley, Berkeley, CA, United States.
³ Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA, United States; Institute for Quantitative Biosciences (QB3), University of California, Berkeley, Berkeley, CA, United States. Electronic address: marqusee@berkeley.edu.
⁴ Department of Chemistry and Biochemistry, University of Oregon, Eugene, OR, United States; Institute of Molecular Biology, University of Oregon, Eugene, OR, United States. Electronic address: harms@uoregon.edu.

Abstract

Were ancient proteins systematically different than modern proteins? The answer to this question is profoundly important, shaping how we understand the origins of protein biochemical, biophysical, and functional properties. Ancestral sequence reconstruction (ASR), a phylogenetic approach to infer the sequences of ancestral proteins, may reveal such trends. We discuss two proposed trends: a transition from higher to lower thermostability and a tendency for proteins to acquire higher specificity over time. We review the evidence for elevated ancestral thermostability and discuss its possible origins in a changing environmental temperature and/or reconstruction bias. We also conclude that there is, as yet, insufficient data to support a trend from promiscuity to specificity. Finally, we propose future work to understand these proposed evolutionary trends.

Publication types

Review
Research Support, N.I.H., Extramural
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, Non-U.S. Gov't

MeSH terms

Animals
Evolution, Molecular
Phylogeny
Protein Stability
Proteins / chemistry*
Proteins / genetics
Proteins / metabolism*
Substrate Specificity
Temperature*

Substances

Proteins

Abstract

Publication types

MeSH terms

Substances

Grants and funding