Identification of major ADH genes in ethanol metabolism of Pichia pastoris

Yeast ◽  
2019 ◽  
Vol 37 (2) ◽  
pp. 227-236
Author(s):  
Mert Karaoğlan ◽  
Fidan Erden‐Karaoğlan ◽  
Semiramis Yılmaz ◽  
Mehmet İnan
Keyword(s):  
Pichia Pastoris ◽  
Ethanol Metabolism ◽  
Adh Genes

scholarly journals Identification and Functional Analysis of ThADH1 and ThADH4 Genes Involved in Tolerance to Waterlogging Stress in Taxodium hybrid ‘Zhongshanshan 406’

Genes ◽  
2021 ◽  
Vol 12 (2) ◽  
pp. 225
Author(s):  
Lei Xuan ◽  
Jianfeng Hua ◽  
Fan Zhang ◽  
Zhiquan Wang ◽  
Xiaoxiao Pei ◽  
...  
Keyword(s):  
Ethanol Metabolism ◽  
Flooding Tolerance ◽  
Transcriptome Data ◽  
Low Oxygen ◽  
Anaerobic Conditions ◽  
Waterlogging Tolerance ◽  
Waterlogging Stress ◽  
Adh Genes ◽  
Oxygen Conditions ◽  
Stems And Leaves

The Taxodium hybrid ‘Zhongshanshan 406’ (T. hybrid ‘Zhongshanshan 406’) [Taxodium mucronatum Tenore × Taxodium distichum (L.). Rich] has an outstanding advantage in flooding tolerance and thus has been widely used in wetland afforestation in China. Alcohol dehydrogenase genes (ADHs) played key roles in ethanol metabolism to maintain energy supply for plants in low-oxygen conditions. Two ADH genes were isolated and characterized—ThADH1 and ThADH4 (GenBank ID: AWL83216 and AWL83217—basing on the transcriptome data of T. hybrid ‘Zhongshanshan 406’ grown under waterlogging stress. Then the functions of these two genes were investigated through transient expression and overexpression. The results showed that the ThADH1 and ThADH4 proteins both fall under ADH III subfamily. ThADH1 was localized in the cytoplasm and nucleus, whereas ThADH4 was only localized in the cytoplasm. The expression of the two genes was stimulated by waterlogging and the expression level in roots was significantly higher than those in stems and leaves. The respective overexpression of ThADH1 and ThADH4 in Populus caused the opposite phenotype, while waterlogging tolerance of the two transgenic Populus significantly improved. Collectively, these results indicated that genes ThADH1 and ThADH4 were involved in the tolerance and adaptation to anaerobic conditions in T. hybrid ‘Zhongshanshan 406’.

Functional analysis of alcohol dehydrogenase (ADH) genes in Pichia pastoris

2015 ◽  
Vol 38 (3) ◽  
pp. 463-469 ◽  
Author(s):  
Mert Karaoglan ◽  
Fidan Erden Karaoglan ◽  
Mehmet Inan
Keyword(s):  
Functional Analysis ◽  
Pichia Pastoris ◽  
Alcohol Dehydrogenase ◽  
Adh Genes

Ethanol metabolism in suspension cultured carrot cells

1991 ◽  
Vol 82 (1) ◽  
pp. 103-108
Author(s):  
P. Perata ◽  
A. Alpi
Keyword(s):  
Ethanol Metabolism ◽  
Carrot Cells

Ethanol Metabolism in Vivo and the Role of Hepatic Microsomal Ethanol Oxidation

1972 ◽  
Vol 33 (3) ◽  
pp. 751-755 ◽  
Author(s):  
Mary K. Roach ◽  
Myrna Khan ◽  
Marguerite Knapp ◽  
W. N. Reese
Keyword(s):  
Ethanol Oxidation ◽  
Ethanol Metabolism

Optimization of fermentation conditions for the production of recombinant hpdgf-bb in Pichia pastoris

2015 ◽  
Vol 37 (1se) ◽  
Author(s):  
Duong Long Duy ◽  
Pham Minh Vu ◽  
Nguyen Tri Nhan ◽  
Tran Linh Thuoc ◽  
Dang Thi Phuong Thao
Keyword(s):  
Pichia Pastoris ◽  
Fermentation Conditions ◽  
Optimization Of Fermentation

Cloning and Expression of Recombinant Human Insulin Gene in Pichia pastoris

2019 ◽  
Vol 10 (01) ◽  
Author(s):  
Rafid A. Abdulkareem
Keyword(s):  
Pichia Pastoris ◽  
Human Insulin ◽  
Expression Vector ◽  
Expression System ◽  
Insulin Gene ◽  
Cloning And Expression ◽  
Pcr Analysis ◽  
Major Band ◽  
Human Insulin Gene ◽  
Pichia Pastoris Expression System

The main goal of the current study was cloning and expression of the human insulin gene in Pichia pastoris expression system, using genetic engineering techniques and its treatment application. Total RNA was purified from fresh normal human pancreatic tissue. RNA of good quality was chosen to obtain a first single strand cDNA. Human preproinsulin gene was amplified from cDNA strand, by using two sets of specific primers contain EcoR1 and Notl restriction sites. The amplified preproinsulin gene fragment was double digested with EcoRI and Not 1 restriction enzymes, then inserted into pPIC9K expression vector. The new pPIC9K-hpi constructive expression vector was transformed by the heat-shock method into the E.coli DH5α competent cells. pPic9k –hpi, which was propagated in the positive transformant E. coli cells, was isolated from cells and then linearised by restriction enzyme SalI, then transformed into Pichia pastoris GS115 using electroporation method. Genomic DNA of His+ transformants cell was extracted and used as a template for PCR analysis. The results showed, that the pPic9k – hpi was successfully integrated into the P. pastoris genome, for selected His+ transformants clones on the anticipated band at 330 bp, which is corresponded to the theoretical molecular size of the human insulin gene. To follow the insulin expression in transformans, Tricine–SDS gel electrophoresis and Western blot analysis were conducted. The results showed a successful expression of recombinant protein was detected by the presence of a single major band with about (5.8 KDa) on the gel. These bands correspond well with the size of human insulin with the theoretical molecular weight (5.8 KDa).

SECRETED EXPRESSION OF LITOPENAEUS VANNAMEI LYSOZYME GENE IN PICHIA PASTORIS AND ITS BIOACTIVITY DETECTION

2010 ◽  
Vol 36 (6) ◽  
pp. 1091-1096
Author(s):  
Shu-Guang BIAN ◽  
Hua-Xin CHEN ◽  
Peng JIANG ◽  
Hai-Bo ZHANG ◽  
Zhao-Pu LIU ◽  
...  
Keyword(s):  
Pichia Pastoris ◽  
Litopenaeus Vannamei ◽  
Lysozyme Gene ◽  
Secreted Expression

CLONING AND EXPRESSION OF SILURUS.MERIDIUNLIS OBESE GENE IN PICHIA. PASTORIS

2008 ◽  
Vol 32 (1) ◽  
pp. 112-115
Author(s):  
Fen NIE
Keyword(s):  
Pichia Pastoris ◽  
Cloning And Expression ◽  
I Gene

Expression and Characteristics of Phytases from Obesumbacterium proteus in Pichia pastoris Yeast

2018 ◽  
Vol 34 (4) ◽  
pp. 18-25 ◽  
Author(s):  
T.L. Gordeeva ◽  
◽  
L.N. Borshchevskaya ◽  
A.N. Kalinina ◽  
S.P. Sineoky ◽  
...  
Keyword(s):  
Pichia Pastoris ◽  
Pichia Pastoris Yeast
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