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Cho, Moo Je
Ulsan National Institute of Science and Technology
Research Interests
  • Calcium Signaling

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Identification of calmodulin isoform-specific binding peptides from a phage-displayed random 22-mer peptide library

Cited 23 times inthomson ciCited 21 times inthomson ci
Title
Identification of calmodulin isoform-specific binding peptides from a phage-displayed random 22-mer peptide library
Author
Choi, JYLee, SHPark, Chan YoungHeo, WDKim, JCKim, MCChung, WSMoon, BCCheong, YHKim, CYYoo, JHKoo, JCOk, HMChi, SWRyu, SELee, SYLim, COCho, Moo Je
Keywords
Protein binding
Issue Date
200206
Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Citation
JOURNAL OF BIOLOGICAL CHEMISTRY, v.277, no.24, pp.21630 - 21638
Abstract
Plants express numerous calmodulin (CaM) isoforms that exhibit differential activation or inhibition of CaM-dependent enzymes in vitro; however, their specificities toward target enzyme/protein binding are uncertain. A random peptide library displaying a 22-mer peptide on a bacteriophage surface was constructed to screen peptides that specifically bind to plant CaM isoforms (soybean calmodulin (ScaM)-1 and SCaM-4 were used in this study) in a Ca2+-dependent manner. The deduced amino acid sequence analyses of the respective 80 phage clones that were independently isolated via affinity panning revealed that SCaM isoforms require distinct amino acid sequences for optimal binding. SCaM-1-binding peptides conform to a 1-5-10 ((FILVW)XXX(FILV) XXXX(FILVW)) motif (where X denotes any amino acid), whereas SCaM-4-binding peptide sequences conform to a 1-8-14 ((FILVW)XXXXXX(FAILVW)XXXXX(FILVW)) motif. These motifs are classified based on the positions of conserved hydrophobic residues. To examine their binding properties further, two representative peptides from each of the SCaM isoform-binding sequences were synthesized and analyzed via gel mobility shift assays, Trp fluorescent spectra analyses, and phosphodiesterase competitive inhibition experiments. The results of these studies suggest that SCaM isoforms possess different binding sequences for optimal target interaction, which therefore may provide a molecular basis for CaM isoform-specific function in plants. Furthermore, the isolated peptide sequences may serve not only as useful CaM-binding sequence references but also as potential reagents for studying CaM isoform-specific function in vivo.
URI
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DOI
http://dx.doi.org/10.1074/jbc.M110803200
ISSN
0021-9258
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