Heterologous transformation of Zalerion arboricola

1994 ◽  
Vol 26 (3) ◽  
pp. 217-224 ◽  
Author(s):  
Rosemarie Kelly ◽  
Elizabeth Register ◽  
Margaret Sosa
Keyword(s):  
Heterologous Transformation

Isolation and heterologous transformation analysis of a pollen-specific promoter from wheat (Triticum aestivum L.)

2009 ◽  
Vol 37 (2) ◽  
pp. 737-744 ◽  
Author(s):  
Ling Chen ◽  
Zhiming Tu ◽  
Javeed Hussain ◽  
Ling Cong ◽  
Yinjun Yan ◽  
...  
Keyword(s):  
Triticum Aestivum ◽  
Triticum Aestivum L ◽  
Heterologous Transformation

scholarly journals Heterologous expression of heat stress-responsive AtPLC9 confers heat tolerance in transgenic rice

2020 ◽  
Vol 20 (1) ◽  
Author(s):  
Yuliang Liu ◽  
Xinye Liu ◽  
Xue Wang ◽  
Kang Gao ◽  
Weiwei Qi ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Heat Stress ◽  
Transgenic Rice ◽  
Heat Tolerance ◽  
Calcium Ion ◽  
Molecular Breeding ◽  
Cereal Crops ◽  
Rna Seq ◽  
Wild Type ◽  
Heterologous Transformation

Abstract Background As global warming becomes increasingly severe, it is urgent that we enhance the heat tolerance of crops. We previously reported that Arabidopsis thaliana PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C9 (AtPLC9) promotes heat tolerance. Results In this study, we ectopically expressed AtPLC9 in rice to examine its potential to improve heat tolerance in this important crop. Whereas AtPLC9 did not improve rice tolerance to salt, drought or cold, transgenic rice did exhibit greater heat tolerance than the wild type. High-throughput RNA-seq revealed extensive and dynamic transcriptome reprofiling in transgenic plants after heat stress. Moreover, the expression of some transcription factors and calcium ion-related genes showed specific upregulation in transgenic rice after heat stress, which might contribute to the enhanced heat tolerance. Conclusions This study provides preliminary guidance for using AtPLC9 to improve heat tolerance in cereal crops and, more broadly, highlights that heterologous transformation can assist with molecular breeding.

scholarly journals Heterologous transformation ofCochliobolus lunatus

1991 ◽  
Vol 77 (2-3) ◽  
pp. 145-150 ◽  
Author(s):  
Marina Dermastia ◽  
Damjana Rozman ◽  
Radovan Komel
Keyword(s):  
Heterologous Transformation

Heterologous transformation ofClaviceps purpurea

1989 ◽  
Vol 11 (6) ◽  
pp. 389-392 ◽  
Author(s):  
Aleksandra Comino ◽  
Margareta Kolar ◽  
Helmut Schwab ◽  
Helena Sočič
Keyword(s):  
Heterologous Transformation

Transformation of Penicillium griseoroseum nitrate reductase mutant with the nia gene from Fusarium oxysporum

1998 ◽  
Vol 44 (5) ◽  
pp. 487-489 ◽  
Author(s):  
Marisa V de Queiroz ◽  
Andréa O Barros ◽  
Everaldo G de Barros ◽  
Walter V Guimarães ◽  
Elza F de Araújo
Keyword(s):  
Nitrate Reductase ◽  
Fusarium Oxysporum ◽  
Structural Gene ◽  
Dna Hybridization ◽  
Transformation System ◽  
Genetic Studies ◽  
Penicillium Griseoroseum ◽  
Heterologous Transformation ◽  
Tandem Arrays

A heterologous transformation system for Penicillium griseoroseum has been developed. This system is based on nia, the structural gene from Fusarium oxysporum encoding nitrate reductase. Penicillium griseoroseum niaD mutants have been selected from chlorate-resistant colonies. Among 24 chlorate-resistant colonies analyzed, 2 were confirmed to be niaD mutants. Transformation frequencies of 8 transformants/µg of DNA were obtained. DNA hybridization analyses of five transformants showed distinct integration patterns of the plasmid and in all of them the integration occurred at tandem arrays. The transformation system established in this work will be useful for genetic studies of the pectinolytic complex genes from P. griseoroseum.Key words: Penicillium griseoroseum, heterologous transformation, nitrate reductase.

scholarly journals Identification and Analysis of the Polyhydroxyalkanoate-Specific β-Ketothiolase and Acetoacetyl Coenzyme A Reductase Genes in the Cyanobacterium Synechocystis sp. Strain PCC6803

2000 ◽  
Vol 66 (10) ◽  
pp. 4440-4448 ◽  
Author(s):  
Gaspar Taroncher-Oldenburg ◽  
Koren Nishina ◽  
Gregory Stephanopoulos
Keyword(s):  
Sequence Analysis ◽  
Coenzyme A ◽  
Dry Weight ◽  
Growth Conditions ◽  
Open Reading Frames ◽  
Pha Synthase ◽  
Promoter Regions ◽  
Short Chain Length ◽  
Heterologous Transformation ◽  
Coa Reductase

ABSTRACT Synechocystis sp. strain PCC6803 possesses a polyhydroxyalkanoate (PHA)-specific β-ketothiolase encoded byphaASyn and an acetoacetyl-coenzyme A (CoA) reductase encoded by phaBSyn . A similarity search of the entire Synechocystis genome sequence identified a cluster of two putative open reading frames (ORFs) for these genes, slr1993 and slr1994. Sequence analysis showed that the ORFs encode proteins having 409 and 240 amino acids, respectively. The two ORFs are colinear and most probably coexpressed, as revealed by sequence analysis of the promoter regions. Heterologous transformation of Escherichia coli with the two genes and the PHA synthase of Synechocystis resulted in accumulation of PHAs that accounted for up to 12.3% of the cell dry weight under high-glucose growth conditions. Targeted disruption of the above gene cluster inSynechocystis eliminated the accumulation of PHAs. ORFs slr1993 and slr1994 thus encode the PHA-specific β-ketothiolase and acetoacetyl-CoA reductase of Synechocystis and, together with the recently characterized PHA synthase genes in this organism (S. Hein, H. Tran, and A. Steinbüchel, Arch. Microbiol. 170:162–170, 1998), form the first complete PHA biosynthesis pathway known in cyanobacteria. Sequence alignment of all known short-chain-length PHA-specific acetoacetyl-CoA reductases also suggests an extended signature sequence, VTGXXXGIG, for this group of proteins. Phylogenetic analysis further places the origin ofphaASyn and phaBSyn in the γ subdivision of the division Proteobacteria.

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