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Related Experiment Videos

Structural requirements for alpha-mating factor activity

G Houen1, O Nielsen, C Flanagan

  • 1Department of Autoimmunology, Statens Seruminstitut, Copenhagen, Denmark.

FEBS Letters
|August 5, 1996
PubMed
Summary
This summary is machine-generated.

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Luteinizing hormone-releasing hormone (LHRH) does not exhibit alpha-mating factor (alpha-MF) activity in yeast. Structural analysis of hybrid peptides reveals that an intact C-terminus and specific spacing are crucial for alpha-MF activity.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Endocrinology

Background:

  • Saccharomyces cerevisiae alpha-mating factor (alpha-MF) shares structural homology with mammalian luteinizing hormone-releasing hormone (LHRH).
  • Previous studies indicated alpha-MF exhibits LHRH activity, but the converse was unconfirmed.

Purpose of the Study:

  • To investigate whether LHRH possesses alpha-MF activity in yeast.
  • To elucidate the structural determinants of alpha-MF and LHRH activities through synthesis and testing of hybrid peptides.

Main Methods:

  • Synthesis of hybrid peptides combining sequences of alpha-MF and LHRH.
  • Assay of alpha-MF and LHRH activities of synthesized peptides in yeast models.

Main Results:

Related Experiment Videos

  • LHRH did not exhibit alpha-MF activity in yeast.
  • The C-terminal tetrapeptide of alpha-MF was essential for its activity.
  • Insertion of a serine residue at position 4, as in LHRH, abolished alpha-MF activity.
  • Hybrid peptides displayed reduced LHRH activity compared to native hormones.
  • Conclusions:

    • Alpha-MF activity requires an intact C-terminus and precise spacing between N-terminal residues and the C-terminus.
    • Structural homology between alpha-MF and LHRH does not necessarily imply an evolutionary relationship.