1998 Fiscal Year Final Research Report Summary
response to high-salt stress in Halophyte cells
| Project/Area Number |
09660013
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
作物学
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| Research Institution | Kobe University |
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Principal Investigator |
YASUDA Takeshi Kobe University, Faculty of Agriculture, Professor, 農学部, 教授 (20026553)
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| Co-Investigator(Kenkyū-buntansha) |
AZUMA Tetsushi Kobe University, The Graduate School of Science & Technology, Assistant Professo, 自然科学研究科, 助手 (30231913)
UCHIDA Naotsugu Kobe University, Faculty of Agriculture, Associate Professor, 農学部, 助教授 (70151884)
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| Project Period (FY) |
1997 – 1998
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| Keywords | salt stress / Atriplex / Halophyte / cultured cell / germin-like protein |
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| Research Abstract |
Halophyte plants are able to grow under high saline environments. For examining cellular response of Halophyte cells to salt stress, cultured cells from 3 Atriplex species ; 1 entiformis (AL), halimus (AH) and halimus (AH) were treated with and without 0.2M NaCl, and polypeptide patterns were analyzed by 2-D electrophoresis. Significant increase of polypeptide spot were detected in insoluble protein fractions of salt treated Atriplex cells on NEPHGE/SDS electrophoresis. A polypeptide named SP1 was with a molecular mass of 27 kDa with pI over 8.5. The polypeptide was glycoprotein with Con A binding activity. Eluted proteins from electrophoretic spot of LH were used for antibody preparation by mice and N-terminal amino acid sequencing. mRNA were isolated from salt-treated LH cells and cDNA library was prepared, and library screening were done using a probe, which amplified by PCR on primers constructed from N-terminal amino-acid sequences. We have determined the nucleotide sequence of a full length cDNA for SP1 and submitted on the DDBJ/EMBL/GenBank databases (AB024338). Reduced amino acid sequences reveals that SP1 is 224-AA, 24 kDa and pI=9.72. A search of the GenBank data base for SP1 amino acid sequence showed similarity to Germin and oxalate-oxidase.
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