Calmodulin-binding protein BP-10, a probable new member of plant nonspecific lipid transfer protein superfamily

Hua Liu, Ling Xue, Cuifeng Li, Ren Zhang, Qilang Ling

Research output: Contribution to journalArticle

Abstract

CaMBP-10 is a novel plant endogenous calmodulin-binding protein with important physiological functions. The partial cDNA sequence of this protein was cloned using RT-PCR. The deduced peptide (designated PCBP10) is composed of 74 amino acid residues containing a basic amphiphilic α-helix typical for calmodulin-binding proteins. PCBP10 shows very high amino acid sequence homology with plant non-specific lipid-transfer proteins (nsLTPs). Sequence analysis also reveals that PCBP10 has similar amino acid composition to plant nsLTPs, and seven of the eight conserved cysteine residues are found in PCBP10. Furthermore, the secondary structure features of PCBP10 are very similar to those of plant nsLTPs. In addition, there are striking resemblances between CaMBP-10 and plant nsLTPs in their biochemical and physical properties. Our results suggest that CaMBP-10 is a novel member of the plant and nsLTP gene family, and the Ca2+/CaM regulative system may also play roles in lipid metabolism, defense reactions, and the adaptation of plants to natural environment.

Original languageEnglish (US)
Pages (from-to)633-638
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume285
Issue number3
DOIs
StatePublished - Jan 1 2001
Externally publishedYes

Keywords

  • Calmodulin
  • Calmodulin-binding protein
  • Nonspecific lipid-transfer protein

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Calmodulin-binding protein BP-10, a probable new member of plant nonspecific lipid transfer protein superfamily'. Together they form a unique fingerprint.

  • Cite this