The Saccharomyces cerevisiae enolase-related regions encode proteins that are active enolases
Article first published online: 28 JAN 2013
Copyright © 2012 John Wiley & Sons, Ltd.
Volume 30, Issue 2, pages 55–69, February 2013
How to Cite
Kornblatt, M. J., Richard Albert, J., Mattie, S., Zakaib, J., Dayanandan, S., Hanic-Joyce, P. J. and Joyce, P. B. M. (2013), The Saccharomyces cerevisiae enolase-related regions encode proteins that are active enolases. Yeast, 30: 55–69. doi: 10.1002/yea.2940
- Issue published online: 4 FEB 2013
- Article first published online: 28 JAN 2013
- Accepted manuscript online: 27 DEC 2012 08:36PM EST
- Manuscript Accepted: 11 DEC 2012
- Manuscript Received: 9 OCT 2012
- Discovery. Grant Number: 121664
- Natural Sciences and Engineering Research Council of Canada (to P.B.M.J.)
- Saccharomyces cerevisiae;
- enolase-related regions
In addition to two genes (ENO1 and ENO2) known to code for enolase (EC18.104.22.168), the Saccharomyces cerevisiae genome contains three enolase-related regions (ERR1, ERR2 and ERR3) which could potentially encode proteins with enolase function. Here, we show that products of these genes (Err2p and Err3p) have secondary and quaternary structures similar to those of yeast enolase (Eno1p). In addition, Err2p and Err3p can convert 2-phosphoglycerate to phosphoenolpyruvate, with kinetic parameters similar to those of Eno1p, suggesting that these proteins could function as enolases in vivo. To address this possibility, we overexpressed the ERR2 and ERR3 genes individually in a double-null yeast strain lacking ENO1 and ENO2, and showed that either ERR2 or ERR3 could complement the growth defect in this strain when cells are grown in medium with glucose as the carbon source. Taken together, these data suggest that the ERR genes in Saccharomyces cerevisiae encode a protein that could function in glycolysis as enolase. The presence of these enolase-related regions in Saccharomyces cerevisiae and their absence in other related yeasts suggests that these genes may play some unique role in Saccharomyces cerevisiae. Further experiments will be required to determine whether these functions are related to glycolysis or other cellular processes. Copyright © 2012 John Wiley & Sons, Ltd.