2005 Fiscal Year Final Research Report Summary
Studies on the principle of protein architecture by the simplification of amino acid sequence
| Project/Area Number |
16370074
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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 |
Biophysics
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| Research Institution | NARA INSTITUTE OF SCIENCE AND TECHNOLOGY |
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Principal Investigator |
KATAOKA Mikio NARA INSTITUTE OF SCIENCE AND TECHNOLOGY, GRADUATE SCHOOL OF MATERIALS SCIENCE, PROFESSOR, 物質創成科学研究科, 教授 (30150254)
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| Co-Investigator(Kenkyū-buntansha) |
IMAMOTO Yasushi NARA INSTITUTE OF SCIENCE AND TECHNOLOGY, GRADUATE SCHOOL OF MATERIALS SCIENCE, ASSOCIATE PROFESSOR, 物質創成科学研究科, 助教授 (80263200)
YAMAZAKI Yoichi NARA INSTITUTE OF SCIENCE AND TECHNOLOGY, GRADUATE SCHOOL OF MATERIALS SCIENCE, INSTRUCTOR, 物質創成科学研究科, 助手 (40332770)
KAMIKUBO Hironari NARA INSTITUTE OF SCIENCE AND TECHNOLOGY, GRADUATE SCHOOL OF MATERIALS SCIENCE, INSTRUCTOR, 物質創成科学研究科, 助手 (20311128)
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| Project Period (FY) |
2004 – 2005
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| Keywords | photoactive yellow protein / simplification of sequence / circular dichroism / structure-function relationship / amyloid / chromoprotein / PAS family / β scaffold |
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| Research Abstract |
In order to understand the information encoded in an amino-acid sequence, we have created variants of photoactive yellow protein (PYP) with simplified amino-acid sequences. We simplified the amino-acid sequence of PYP using a simple set of rules to reduce overlapping structural information. The simplified PYP protein (sPYP0), which was composed of only nine species of amino acids (Ser,Val,Asp,Lys,Phe,Met,Gly,Pro, and Cys), showed a completely different structure than the native conformation. Even after the evolutionarily conserved residues were restored in the simplified protein (sPYPI), the PYP variant did not properly fold. Additional restorations of the substituted hydrophobic (sPYPII) or hydrophilic residues (sPYPIII) did not lead to a variant that formed the native structure. sPYPIII only shows the tendency of helical formation by TFE. Partial simplification was successfully performed by creating chimeric proteins composed of combinations of wild-type PYP and sPYPIII. Hybrid mutants containing a wild-type β scaffold adopted native-like structures. In contrast, the hybrid mutants that contained the simplified β scaffold demonstrated a tendency to adopt non-native conformations, suggesting that there is a wealth of information about the formation of the structure in the β scaffold. 5 hydrophobic residues in the β scaffold were identified to be responsible for the structure formation. It is also demonstrated that sPYPII takes amyloid-like fibril structure.
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Research Products
(8 results)
