Molecular Basis of Resistance to <i>s</i>-Triazine Herbicides in <i>Poa annua</i> L. and Its Photosynthetic Properties under Different Light Conditions
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- KUMATA Shuji
- Center for Research on Wild Plants, Utsunomiya University
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- YONEYAMA Koichi
- Center for Research on Wild Plants, Utsunomiya University
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- OGASAWARA Masaru
- Center for Research on Wild Plants, Utsunomiya University
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- TAKEUCHI Yasutomo
- Center for Research on Wild Plants, Utsunomiya University
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- KONNAI Makoto
- Center for Research on Wild Plants, Utsunomiya University
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- NAKAJIMA Yoshihiro
- Graduate School of Biological Science, Nara Institute of Science and Technology
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- NAKANO Takeshi
- The Institute of Physical and Chemical Research (RIKEN)
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- YOSHIDA Shigeo
- The Institute of Physical and Chemical Research (RIKEN)
Bibliographic Information
- Other Title
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- スズメノカタビラの<i>s</i>-トリアジン除草剤抵抗性の分子機構および異なる光条件下における光合成機能
- Molecular Basis of Resistance to s-Triazine Herbicides in Poa annua L. and Its Photosynthetic Properties under Different Light Conditions
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Abstract
A simazine resistant biotype of Poa annua L. was found in a golf course in Shizuoka prefecture, Japan. The biotype was highly resistant to s-triazines, almost equally susceptible to the phenylurea, diuron, and more susceptible to the phenol, dinoseb, than the susceptible biotype both at whole plant and at isolated thylakoid levels. The molecular basis of resistance to s-triazine herbicides in the resistant biotype was identified as a mutation in psb A gene giving rise to the replacement of serine 264 by glycine in the D1 protein of photosystem II (PS II). The resistant biotype showed a reduced capacity of photosynthesis when grown under full-sunlight conditions. However, no differences were observed in photosynthetic performance of susceptible and resistant biotypes when grown under shaded conditions. The resistant biotype also showed increased sensitivity to photoinhibition both at whole plant and at isolated PS II membrane levels, indicating that the increased susceptibility in the resistant biotype to the photoinhibition is due to the substitution of serine 264 to glycine in the D1 protein.
Journal
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- Journal of Pesticide Science
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Journal of Pesticide Science 26 (3), 236-243, 2001
Pesticide Science Society of Japan
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Details 詳細情報について
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- CRID
- 1390282680187584000
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- NII Article ID
- 110001713895
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- NII Book ID
- AN00196227
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- ISSN
- 03851559
- 13490923
- 1348589X
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- NDL BIB ID
- 5888909
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- Data Source
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- JaLC
- IRDB
- NDL
- Crossref
- NDL-Digital
- CiNii Articles
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- Abstract License Flag
- Disallowed