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Distant cousins: genomic and sequence diversity within the BPI fold-containing (BPIF)/PLUNC protein family

Colin D Bingle1, Lynne Bingle, C Jeremy Craven

  • 1Academic Unit of Respiratory Medicine, Department of Infection and Immunity, University of Sheffield, Sheffield S10 2JF, UK. c.d.bingle@sheffield.ac.uk

Biochemical Society Transactions
|July 27, 2011
PubMed

Insights

Palate, lung, and nasal epithelium clone (PLUNC) proteins are rapidly evolving lipid-transfer proteins. Their rapid evolution and gene family dynamics challenge traditional definitions, indicating significant functional adaptations.

Area of Science:

  • Biochemistry
  • Evolutionary Biology
  • Genomics

Background:

  • Palate, lung, and nasal epithelium clone (PLUNC) proteins represent the largest group within the bactericidal/permeability-increasing protein/lipopolysaccharide-binding protein family.
  • PLUNC proteins are among the fastest-evolving mammalian protein families, characterized by low sequence similarity and dynamic gene gain/loss across species.

Purpose of the Study:

  • To investigate the evolutionary dynamics of PLUNC proteins and their impact on protein family definitions.
  • To understand how evolutionary forces shape the conserved domains of PLUNC proteins.

Main Methods:

  • Comparative genomics analysis of vertebrate genomes.
  • Examination of gene structure, including exon number/size, protein size, and genomic location.
  • Analysis of conserved disulfide bonds within PLUNC protein domains.

Main Results:

  • PLUNC proteins exhibit rapid evolution, with significant species-specific gene acquisition and loss.
  • Many vertebrate genes classified outside the traditional PLUNC definition show variations in conserved features like exon structure and protein size.
  • These variations suggest ongoing evolutionary pressures acting on functionally important conserved domains.

Conclusions:

  • The definition of the PLUNC protein family requires re-evaluation due to extensive evolutionary divergence.
  • Evolutionary forces actively modify the structure of conserved domains in PLUNC proteins, likely for functional adaptation.
  • Further research is needed to fully elucidate the functional implications of these evolutionary changes in PLUNC proteins.

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