Chapter 8 Flashcards
Overview of Regulation
Cells metabolically complex.
Cells need to change metabolic activities to adjust:
-phase of cell cycle
-environmental conditions
-presence of organisms
Metabolism requires enzymes that must be present and functional.
Major modes of regulation
Gene expression- transcription followed by translation.
Most proteins are enzymes that carry out biochemical reactions.
Constitutive proteins needed at same level.
Microbial genomes encode many proteins not needed always.
Two major levels of regulation in cells
Control activity of preexisting enzymes: -post translational regulation -very rapid Control amount of enzyme: -regulate level of transcription -regulate translation -slow
Constitutive enzymes
Catalyze metabolic reactions that constantly occur:
-independent of growth conditions
-independent of cell cycle
Ex. pyruvate decarboxylase (Kreb’s)
Regulating an enzyme that already exists
Post translational regulation, happens after protein is made.
2 major strategies for post translational regulation:
-feedback inhibition
-covalent modification
Feedback inhibition
Molecules in cell bind to enzyme and inactivate it.
Binding reversible when conditions change.
Used in biosynthetic pathways. (amino acid synthesis).
Often first enzyme is inhibited by end product.
Feedback Inhibition: Allostery
Allosteric enzymes have 2 binding sites:
- Active site which binds substrate and catalyzes metabolic reaction.
- Allosteric site which binds inhibitor.
Allostery: Inhibitor binds allosteric site:
- shape of enzyme changes, including active site.
- Substrate no longer fits in active site.
- Binding reversible.
Covalent modification
Adds or removes small molecule. Frequent examples involve: -phosphate groups -methyl groups Molecule is covalently bound to enzyme.
Enzyme production method: DNA binding proteins
mRNA has short half life:
-prevents production of unneeded proteins.
Regulation of transcription often requires proteins that bind DNA.
Small molecules influence binding of regulatory proteins to DNA:
-proteins regulate transcription.
DNA binding proteins
DNA binding proteins interact with DNA in sequence specific manner
-phosphate backbone of DNA
Major groove of DNA main site of protein binding
Inverted repeats frequently binding site for regulatory proteins.
DNA binding protein structures
Homodimeric proteins: proteins composed of two identical polypeptides.
Protein dimers interact with inverted repeats on DNA.
-Each polypeptide binds to one inverted repeat.
DNA binding protein structures: helix turn helix
First helix recognition helix.
Second helix stabilizing helix.
Many different DNA-binding proteins from bacteria contain helix turn helix.
DNA binding protein structures: Zinc finger
Protein structure that binds zinc ion.
Typically two or three zinc fingers on proteins that use them for DNA binding.
DNA binding protein structures: Leucine zipper
Leucine residues spaced every seven amino acids.
Does not interact directly with DNA .