Functional analysis of active amino acid residues of the mercaptosuccinate dioxygenase of Variovorax paradoxus B4

2019 ◽  
Vol 120 ◽  
pp. 61-68 ◽  
Author(s):  
Ulrike Brandt ◽  
Gulsina Galant ◽  
Christina Meinert-Berning ◽  
Alexander Steinbüchel
Keyword(s):  
Functional Analysis ◽  
Amino Acid ◽  
Amino Acid Residues ◽  
Variovorax Paradoxus ◽  
Active Amino Acid

Functional analysis of polar amino-acid residues in membrane associated regions of the NHE1 isoform of the mammalian Na+ /H+ exchanger

2001 ◽  
Vol 268 (17) ◽  
pp. 4674-4685 ◽  
Author(s):  
Rakhilya Murtazina ◽  
Brenda J. Booth ◽  
Bonnie L. Bullis ◽  
Dyal N. Singh ◽  
Larry Fliegel
Keyword(s):  
Functional Analysis ◽  
Amino Acid ◽  
Amino Acid Residues ◽  
Polar Amino Acid

scholarly journals Molecular Characterization and Functional Analysis of a Necrosis- and Ethylene-Inducing, Protein-Encoding Gene Family from Verticillium dahliae

2012 ◽  
Vol 25 (7) ◽  
pp. 964-975 ◽  
Author(s):  
Bang-Jun Zhou ◽  
Pei-Song Jia ◽  
Feng Gao ◽  
Hui-Shan Guo
Keyword(s):  
Functional Analysis ◽  
Amino Acid ◽  
Verticillium Dahliae ◽  
Defense Responses ◽  
Phytopathogenic Fungus ◽  
Amino Acid Residues ◽  
Wide Range ◽  
Protein Encoding ◽  
Necrotrophic Stage ◽  
Verticillium Dahliae Kleb

Verticillium dahliae Kleb. is a hemibiotrophic, phytopathogenic fungus that causes wilt disease in a wide range of crops, including cotton. Successful host colonization by hemibiotrophic pathogens requires the induction of plant cell death to provide the saprophytic nutrition for the transition from the biotrophic to the necrotrophic stage. In this study, we identified a necrosis-inducing Phytophthora protein (NPP1) domain–containing protein family containing nine genes in a virulent, defoliating isolate of V. dahliae (V592), named the VdNLP genes. Functional analysis demonstrated that only two of these VdNLP genes, VdNLP1 and VdNLP2, encoded proteins that were capable of inducing necrotic lesions and triggering defense responses in Nicotiana benthamiana, Arabidopsis, and cotton plants. Both VdNLP1 and VdNLP2 induced the wilting of cotton seedling cotyledons. However, gene-deletion mutants targeted by VdNLP1, VdNLP2, or both did not affect the pathogenicity of V. dahliae V592 in cotton infection. Similar expression and induction patterns were found for seven of the nine VdNLP transcripts. Through a comparison of the conserved amino acid residues of VdNLP with different necrosis-inducing activities, combined with mutagenesis-based analyses, we identified several novel conserved amino acid residues, in addition to the known conserved heptapeptide GHRHDWE motif and the cysteine residues of the NPP domain–containing protein, that are indispensable for the necrosis-inducing activity of the VdNLP2 protein.

scholarly journals Functional Analysis of Amino Acid Residues Constituting the dNTP Binding Pocket of HIV-1 Reverse Transcriptase

1998 ◽  
Vol 273 (50) ◽  
pp. 33624-33634 ◽  
Author(s):  
Dylan Harris ◽  
Neerja Kaushik ◽  
Pradeep K. Pandey ◽  
Prem N. S. Yadav ◽  
Virendra N. Pandey
Keyword(s):  
Functional Analysis ◽  
Amino Acid ◽  
Reverse Transcriptase ◽  
Binding Pocket ◽  
Amino Acid Residues ◽  
Dntp Binding ◽  
Hiv 1

Functional Analysis of Amino Acid Residues Essential for Activity in the Na+/H+Exchanger of Fission Yeast†

Biochemistry ◽  
1998 ◽  
Vol 37 (23) ◽  
pp. 8282-8288 ◽  
Author(s):  
Pavel Dibrov ◽  
Paul G. Young ◽  
Larry Fliegel
Keyword(s):  
Functional Analysis ◽  
Amino Acid ◽  
Fission Yeast ◽  
Amino Acid Residues

scholarly journals Identification of Amino Acid Residues in the Catalytic Domain of RNase E Essential for Survival of Escherichia coli: Functional Analysis of DNase I Subdomain

Genetics ◽  
2008 ◽  
Vol 179 (4) ◽  
pp. 1871-1879 ◽  
Author(s):  
Eunkyoung Shin ◽  
Hayoung Go ◽  
Ji-Hyun Yeom ◽  
Miae Won ◽  
Jeehyeon Bae ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Functional Analysis ◽  
Amino Acid ◽  
Catalytic Domain ◽  
Dnase I ◽  
Amino Acid Residues ◽  
Rnase E
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