You are currently viewing the abstract.
View Full TextLog in to view the full text
AAAS login provides access to Science for AAAS members, and access to other journals in the Science family to users who have purchased individual subscriptions.
More options
Download and print this article for your personal scholarly, research, and educational use.
Buy a single issue of Science for just $15 USD.
Polymerization regulates hexokinase activity
The yeast hexokinase Glk1 is an actin-fold protein that forms polymers in response to binding its substrates and products. Stoddard et al. now show that Glk1 polymers are structurally distinct from actin filaments and suggest that polymerization of Glk1 evolved independently of the polymerization of other actin-like polymers. Glk1 polymerization inhibits its hexokinase activity, and the monomerpolymer equilibrium appears to set a maximum rate for the entire enzyme pool rather than a maximum rate per enzyme. This inhibition was found to be important for cell viability in the context of nutrient shifts, allowing yeast cells to modulate their metabolism rapidly in response to stochastic changes in the environment.
Science, this issue p. 1039
Abstract
The actin fold is found in cytoskeletal polymers, chaperones, and various metabolic enzymes. Many actin-fold proteins, such as the carbohydrate kinases, do not polymerize. We found that Glk1, a Saccharomyces cerevisiae glucokinase, forms two-stranded filaments with ultrastructure that is distinct from that of cytoskeletal polymers. In cells, Glk1 polymerized upon sugar addition and depolymerized upon sugar withdrawal. Polymerization inhibits enzymatic activity; the Glk1 monomer-polymer equilibrium sets a maximum rate of glucose phosphorylation regardless of Glk1 concentration. A mutation that eliminated Glk1 polymerization alleviated concentration-dependent enzyme inhibition. Yeast containing nonpolymerizing Glk1 were less fit when growing on sugars and more likely to die when refed glucose. Glk1 polymerization arose independently from other actin-related filaments and may allow yeast to rapidly modulate glucokinase activity as nutrient availability changes.
This is an article distributed under the terms of the Science Journals Default License.
