The biochemistry of oleate induction: transcriptional upregulation and peroxisome proliferation

Biochim Biophys Acta. 2006 Dec;1763(12):1392-402. doi: 10.1016/j.bbamcr.2006.07.011. Epub 2006 Jul 26.

Abstract

Unicellular organisms such as yeast constantly monitor their environment and respond to nutritional cues. Rapid adaptation to ambient changes may include modification and degradation of proteins; alterations in mRNA stability; and differential rates of translation. However, for a more prolonged response, changes are initiated in the expression of genes involved in the utilization of energy sources whose availability constantly fluctuates. For example, in the presence of oleic acid as a sole carbon source, yeast cells induce the expression of a discrete set of enzymes for fatty acid beta-oxidation as well as proteins involved in the expansion of the peroxisomal compartment containing this process. In this review chapter, we discuss the factors regulating oleate induction in Saccharomyces cerevisiae, and we also deal with peroxisome proliferation in other organisms, briefly mentioning fatty acid-independent signals that can trigger this process.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Chromatin Assembly and Disassembly
  • DNA-Binding Proteins / metabolism
  • Glucose / metabolism
  • Ligands
  • Mitosporic Fungi / metabolism
  • Oleic Acids / biosynthesis*
  • Peroxisomes / physiology*
  • Pichia / metabolism
  • Protein Conformation
  • Protein-Serine-Threonine Kinases / metabolism
  • Response Elements
  • Saccharomyces cerevisiae / metabolism*
  • Saccharomyces cerevisiae Proteins / chemistry
  • Saccharomyces cerevisiae Proteins / metabolism
  • Transcription Factors / chemistry
  • Transcription Factors / metabolism
  • Transcription, Genetic
  • Up-Regulation

Substances

  • ADR1 protein, S cerevisiae
  • DNA-Binding Proteins
  • Ligands
  • Oleic Acids
  • PIP2 protein, S cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Transcription Factors
  • SNF1-related protein kinases
  • Protein-Serine-Threonine Kinases
  • Glucose