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Heterotrimeric G protein α subunit is involved in rice brassinosteroid response

Cell Research 2006年第12期16卷 916-922页

作者： Lei Wang~(1,2) Yun-Yuan Xu~1 Qi-Bin Ma~(1,2) Dan Li~(1,2) Zhi-Hong Xu~(1,3) Kang Chong~(1,3) 1 Key Laboratory of Photosynthesis and Environmental Molecular Physiology,Institute of Botany,Chinese Academy of Sciences,Nanxincun 20,Xiangshan,Beijing 100093,China,2 Graduate School of the Chinese Academv of Sciences,100046 Beijing,China 3 National Plant Gene Research Center (Beijing),Beijing 100093,China KeyLaboratoryofPhotosynthesisandEnvironmentalMolecularPhysiology InstituteofBotanyChineseAcademyofSciencesNanxincun20XiangshanBeijing100093China GraduateSchooloftheChineseAcademyofSciences 100046BeijingChina

Heterotrimeric G proteins are known to function as messengers in numerous signal transduction *** nullmutation of RGA(rice heterotrimeric G protein α subunit),which encodes the α subunit of heterotrimeric G proteinin rice,causes severe dwarfism and reduced responsiveness to gibberellic acid in ***,less is known aboutheterotrimeric G protein in brassinosteroid(BR)signaling,one of the well-understood phytohormone *** thepresent study,we used root elongation inhibition assay,lamina inclination assay and coleoptile elongation analysis todemonstrated reduced sensitivity of dl mutant plants(caused by the null mutation of RGA)to 24-epibrassinolide(24-epiBL),which belongs to brassinosteroids and plays a wide variety of roles in plant growth and ***,RGA transcript level was decreased in 24-epiBL-treated seedlings in a dose-dependent *** results show thatRGA is involved in rice brassinosteroid response,which may be beneficial to elucidate the molecular mechanisms of Gprotein signaling and provide a novel perspective to understand BR signaling in higher plants.

关键词： heterotrimeric G protein α subunit dl mutant BR signaling rice

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Cloning and Sequence of Nicotinic Acetylcholine Receptor α subunit from Chilo suppressalis

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Zoological Research 2002年第1期23卷 7-13页

作者：韩招久韩召军南京农业大学农业部病虫监测与治理重点开放实验室江苏南京210095

Nicotinic acetylcholine receptors (nAChRs) play a significant role in excitatory synaptic transmission in insects and are the target for chloronicotinyl and nereistoxin *** recent years,Chilo suppressalis,an economically important pest of rice,developed high resistance against monosultap,a nereistoxin insecticide acting on *** order to reveal the hypothesized target insensitive mechanism,studies on the molecular property of nAChR from Chilo suppressalis are *** this study,the full length cDNA of nAChR α subunit from this pest was cloned by *** analysis shows that it is a novel nAChR α subunit,which was named as Cs α 1(Genbank accession ***418987).It contains 1?997?bp nucleotides and involves an open reading frame (ORF) encoding a mature protein of 509 amino acids excluding a signal peptide of 24 amino *** deduced amino acid sequence was 52%-94% identical to the reported insect nAChR genes.

关键词： Chilo suppressalis Gene cloning Nicotinic acetylcholine receptor α subunit

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Bioinformatics Analysis on α subunit Gene of Phycobiliprotein from Spirulina maxima

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Agricultural Science & Technology 2010年第4期11卷 86-89页

作者：刘士伟刘杰李博生北京林业大学生物科学与技术学院北京100083 北京林业大学螺旋藻研究所北京100083

[Objective]The α subunit gene of phycobiliprotein from Spirulina maxima was studied in order to provide a basis for the subsequent study of phycobiliprotein.[Method] Amino acids composition,signal peptides,hydrophobicity/hydrophilicity and trails-membrane topological structure of α subunit gene of phycobiliprotein from Spirulina maxima which registered in GenBank（GenBank AF441177） were analyzed and predicted by the tools of bioinformatic ***,phylogenetic tree was constructed based on α subunit gene of phycobiliprotein from Spirulina maxima,and its molecular evolution was also analyzed.[Result]The phycobiliprotein was rich in amino acids,which not only contained 18 kinds of essential amino acids,but also contained some non-essential amino acids like glycine,aspartic acid,etc.;Analysis on signal peptides and trails-membrane topological structure showed that the phycobiliprotein belonged to intracellular protein;Analysis on hydrophobicity/hydrophilicity showed that the phycobiliprotein belonged to hydrophilic protein;Phylogenetic analysis showed that the phycobiliprotein had a high homology with Arthrospira,which reached 99%-100%.[Conclusion]The study provided a certain reference for studying the relationship and interaction between α subunit and β subunit.

关键词： Phycobiliprotein α subunit Bioinformatics

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