Cutting edge structural protein from the jaws of Nereis virens.
The fang-like jaws of the marine polychaete Nereis virens possess remarkable mechanical properties considering their high protein content and lack of mineralization. Hardness and stiffness properties in the jaw tip are comparable to human dentin and are achieved by extensive coordination of Zn (2+) by a histidine-rich protein framework. In the present study, the predominant protein in the jaw tip, Nvjp-1, was purified and characterized by partial peptide mapping and molecular cloning of a partial cDNA from a jaw pulp library. The deduced amino acid sequence revealed an approximately 38 kDa histidine-rich protein rich in glycine and histidine (approximately 36 and 27%, respectively) with no well-defined repetitive motifs. The effects of pH and metal treatment on aggregation, secondary structure, and hydrodynamic properties of recombinant Nvjp-1 are described. Notably, Zn treatment induced the formation of amyloid-like fibers.
Broomell
Chris C
CC
University of California at Santa Barbara, Santa Barbara, California 93106, USA. broomell@lifesci.ucsb.edu
Chase
Sue F
SF
Laue
Tom
T
Waite
J Herbert
JH
D000595:Amino Acid Sequence; D000682:Amyloid / Q000737:chemistry; D000818:Animals; D003001:Cloning, Molecular; D015723:Gene Library; D005998:Glycine / Q000737:chemistry; D006639:Histidine / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D007568:Jaw / Q000737:chemistry; D018625:Microscopy, Atomic Force; D008969:Molecular Sequence Data; D010449:Peptide Mapping; D011077:Polychaeta / Q000737:chemistry*; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000096:biosynthesis; D012995:Solubility; D017550:Spectroscopy, Fourier Transform Infrared; D015032:Zinc / Q000737:chemistry
D000682:Amyloid; D011994:Recombinant Proteins; D006639:Histidine; D015032:Zinc; D005998:Glycine