2011 Fiscal Year Final Research Report
Molecular mechanism of aragonite crystal formation by proteins from Pteria penguin pearl shell, and its application to the development of functional materials
| Project/Area Number |
20350073
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Chemistry related to living body
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| Research Institution | Tohoku University |
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Principal Investigator |
OGAWA Tomohisa 東北大学, 大学院・生命科学研究科, 准教授 (80240901)
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| Co-Investigator(Renkei-kenkyūsha) |
YOSHIMI Kyosuke 東北大学, 大学院・環境科学研究科, 准教授 (80230803)
SHIRAI Tsuyoshi 長浜バイオ大学, バイオサイエンス学部, 教授 (00262890)
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| Project Period (FY) |
2008 – 2011
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| Keywords | バイオテクノロジー / バイオミネラリゼーション |
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| Research Abstract |
Novel 26 kDa ADP rybosyl transferase-like proteins (ARTL26Ps)and Jacalin-related lectins (JRLs)were isolated from the muntle of Pteria penguin pearl shell. To investigate the molecular mechanisms of ARTL26Ps in biomineralization, we achieved in vitro crystal growth experiments using fluorescent-labeled ARTL26P-1 and-2, resulting these two proteins showed the different distribution and functions although their primary sequences were identical except for only 4 amino acids. ARTL26P-2 promoted the nucleation and increased the number of crystals, while ARTL26P-1 regulated the molphologies of CaCO_3 crystals. Thus the ART-like 26 kDa proteins regulate the aragonite crystal formation via nucleation and growth of aragonite crystals in P. penguin nacre shell. On the other hand, JRLs showed the sequence similarities, interestingly they had quite different carbohydrate binding specificities. Furthermore, CaCO3 crystalization in vitro indicated that PPL2A affected on the biomineralization of Pteria penguin with increasing crystals, while PPL3 inhibited the crystalization.
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