A part of ice nucleation protein exhibits the ice-binding ability.
We generated a recombinant 96-residue polypeptide corresponding to a sequence Tyr176-Gly273 of ice nucleation protein from Pseudomonas syringae (denoted INP96). INP96 exhibited an ability to shape an ice crystal, whose morphology is highly similar to the hexagonal-bipyramid generally identified for antifreeze protein. INP96 also showed a non-linear, concentration-dependent retardation of ice growth. Additionally, circular dichroism and NMR measurements suggested a local structural construction in INP96, which undergoes irreversible thermal denaturation. These data imply that a part of INP constructs a unique structure so as to interact with the ice crystal surfaces.
Kobashigawa
Yoshihiro
Y
Functional Protein Research Group, Research Institute of Genome-based Biofactory, National Institute of Advanced Industrial Science and Technology (AIST), Toyohira, Sapporo 062-8517, Japan.
Nishimiya
Yoshiyuki
Y
Miura
Kazunori
K
Ohgiya
Satoru
S
Miura
Ai
A
Tsuda
Sakae
S
D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D003460:Crystallization; D007053:Ice; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D010446:Peptide Fragments / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D011489:Protein Denaturation; D020673:Protein Renaturation; D044224:Pseudomonas syringae / Q000737:chemistry* / Q000235:genetics; D016415:Sequence Alignment; D013696:Temperature
D001425:Bacterial Outer Membrane Proteins; D007053:Ice; D010446:Peptide Fragments; C063113:ice nucleation protein