1.TRANSFORMATION OF BACILLUS THURINGIENSIS RECIPIENT BMB171 BY ELECTROPORATION
Lin LI ; Zongze SHAO ; Ziniu YU
Microbiology 1992;0(05):-
This paper reports the optimized electro-transformation parameters of Bacillus thuringiensis plasmid-free mutant strain BMB171 by electroporation, and expressing effect of several cry genes introduced in this recipient. It showed that a highest electro-transformation frequency could be obtained, when SG solution was used as the buffer, and a 10.0V/cm of field strength, one time of pulse as well as a growth phase of recipient cells at the exponential phase (OD650nm value was 0.2~0.3) were selected. The highest of electro-transformation frequency with pHT3101 could reach at 8 ?107 hansformants/?g DNA. The transformation frequencies increased at linear velocity as the concentration increase of pHT3101 from 54.69pg/ml to 3.50?g/mL, then reached saturation afterwards. All plasmids introduced in BMB171 could produce characteristic insecticidal crystal proteins through expression of relevent cry genes carried by them. Meanwhile, these insecticidal crystal proteins could form parasporal crystals, which have characteristic geometric shapes.
2.Mechanism and application of molecular self-assembly in Sup35 prion domain of Saccharomyces cerevisiae.
Wen YIN ; Jin HE ; Ziniu YU ; Jieping WANG
Chinese Journal of Biotechnology 2011;27(10):1401-1407
Sup35 in its native state is a translation termination factor in Saccharomyces cerevisiae. The prion domain of Sup35p can form amyloid-like proteinaceous fibrils in vitro and in vivo. Furthermore, the in-register cross beta-sheet structure of Sup35p amyloid fibrils is similar to those formed in other species. Therefore, studies on mechanism of Sup35p self-assembly can be an appropriate model to study protein misfolding-related diseases and prion biology. Because of its ability to self-assemble into nanowires, the prion domain of Sup35p has been widely used in biotechnology and nanotechnology.
Amino Acid Sequence
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Amyloid
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chemistry
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metabolism
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Molecular Sequence Data
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Peptide Termination Factors
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chemistry
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Prions
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chemistry
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Protein Conformation
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Saccharomyces cerevisiae
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genetics
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metabolism
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Saccharomyces cerevisiae Proteins
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chemistry
3.Comparative Genomics Reveals Evolutionary Drivers of Sessile Life and Left-right Shell Asymmetry in Bivalves
Zhang YANG ; Mao FAN ; Xiao SHU ; Yu HAIYAN ; Xiang ZHIMING ; Xu FEI ; Li JUN ; Wang LILI ; Xiong YUANYAN ; Chen MENGQIU ; Bao YONGBO ; Deng YUEWEN ; Huo QUAN ; Zhang LVPING ; Liu WENGUANG ; Li XUMING ; Ma HAITAO ; Zhang YUEHUAN ; Mu XIYU ; Liu MIN ; Zheng HONGKUN ; Wong NAI-KEI ; Yu ZINIU
Genomics, Proteomics & Bioinformatics 2022;(6):1078-1091
Bivalves are species-rich mollusks with prominent protective roles in coastal ecosystems.Across these ancient lineages,colony-founding larvae anchor themselves either by byssus produc-tion or by cemented attachment.The latter mode of sessile life is strongly molded by left-right shell asymmetry during larval development of Ostreoida oysters such as Crassostrea hongkongensis.Here,we sequenced the genome of C.hongkongensis in high resolution and compared it to reference bivalve genomes to unveil genomic determinants driving cemented attachment and shell asymmetry.Importantly,loss of the homeobox gene Antennapedia(Antp)and broad expansion of lineage-specific extracellular gene families are implicated in a shift from byssal to cemented attachment in bivalves.Comparative transcriptomic analysis shows a conspicuous divergence between left-right asymmetrical C.hongkongensis and symmetrical Pinctada fucata in their expression profiles.Especially,a couple of orthologous transcription factor genes and lineage-specific shell-related gene families including that encoding tyrosinases are elevated,and may cooperatively govern asymmet-rical shell formation in Ostreoida oysters.