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Expression Analysis of Dph genes 1-7 under
heat stress in Arabidopsis thaliana

Introduction:

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Diphthamide
is a modified histidine residue that is present in eurkaryotic and archeal
elongation factor 2(eEF2) as a result of post translation modification. Diphthamide
is targeted by diphtheria toxin, produced by Corynebacterium diphtheriae and exotoxin A, produced by Pseudomonas aeruginosa that are involved
in catalyzing the transfer of ADP-ribose from NAD+ to eEF2. eEF2
catalyzes the translocation of mRNA and peptidyl-tRNA from ribosome A site to P
site.

This
ADP ribosylation leads to inactivation of EF2, hence the protein synthesis
ceases and the cell dies (Honjo et al., 1968, Jorgensen et al., 2006).

 

Biosynthesis of Diphthamide:

Biosynthesis of
Diphthamide involves stepwise additions to His715(His669
in yeast) residue of eukaryotic elongation factor 2. Biosynthesis begins with
transfer of the 3-amino-3-carboxypropyl (ACP) group of S-adenosylmethionine(AdoMet)
to the imidazole C-2 of the precursor histidine residue. Trimethylation of newly
formed amino group using AdoMet as a source of methyl group leads to the
formation of Diphthine. Diphthine is converted to Diphthamide by ATP dependent
amidation of carboxyl group. Mutants defective in Diphthamide biosynthesis have
been isolated by selection for resistance to the actions of Diphtheria toxin
and exotoxin A.These mutations are categorized into five complementation groups

 

 

 Expression Analysis of Dph genes 1-7 under
heat stress in Arabidopsis thaliana

Introduction:

Diphthamide
is a modified histidine residue that is present in eurkaryotic and archeal
elongation factor 2(eEF2) as a result of post translation modification. Diphthamide
is targeted by diphtheria toxin, produced by Corynebacterium diphtheriae and exotoxin A, produced by Pseudomonas aeruginosa that are involved
in catalyzing the transfer of ADP-ribose from NAD+ to eEF2. eEF2
catalyzes the translocation of mRNA and peptidyl-tRNA from ribosome A site to P
site.

This
ADP ribosylation leads to inactivation of EF2, hence the protein synthesis
ceases and the cell dies (Honjo et al., 1968, Jorgensen et al., 2006).

 

Biosynthesis of Diphthamide:

Biosynthesis of
Diphthamide involves stepwise additions to His715(His669
in yeast) residue of eukaryotic elongation factor 2. Biosynthesis begins with
transfer of the 3-amino-3-carboxypropyl (ACP) group of S-adenosylmethionine(AdoMet)
to the imidazole C-2 of the precursor histidine residue. Trimethylation of newly
formed amino group using AdoMet as a source of methyl group leads to the
formation of Diphthine. Diphthine is converted to Diphthamide by ATP dependent
amidation of carboxyl group. Mutants defective in Diphthamide biosynthesis have
been isolated by selection for resistance to the actions of Diphtheria toxin
and exotoxin A.These mutations are categorized into five complementation groups

 

 

 

 Expression Analysis of Dph genes 1-7 under
heat stress in Arabidopsis thaliana

Introduction:

Diphthamide
is a modified histidine residue that is present in eurkaryotic and archeal
elongation factor 2(eEF2) as a result of post translation modification. Diphthamide
is targeted by diphtheria toxin, produced by Corynebacterium diphtheriae and exotoxin A, produced by Pseudomonas aeruginosa that are involved
in catalyzing the transfer of ADP-ribose from NAD+ to eEF2. eEF2
catalyzes the translocation of mRNA and peptidyl-tRNA from ribosome A site to P
site.

This
ADP ribosylation leads to inactivation of EF2, hence the protein synthesis
ceases and the cell dies (Honjo et al., 1968, Jorgensen et al., 2006).

 

Biosynthesis of Diphthamide:

Biosynthesis of
Diphthamide involves stepwise additions to His715(His669
in yeast) residue of eukaryotic elongation factor 2. Biosynthesis begins with
transfer of the 3-amino-3-carboxypropyl (ACP) group of S-adenosylmethionine(AdoMet)
to the imidazole C-2 of the precursor histidine residue. Trimethylation of newly
formed amino group using AdoMet as a source of methyl group leads to the
formation of Diphthine. Diphthine is converted to Diphthamide by ATP dependent
amidation of carboxyl group. Mutants defective in Diphthamide biosynthesis have
been isolated by selection for resistance to the actions of Diphtheria toxin
and exotoxin A.These mutations are categorized into five complementation groups

 

 

 

 

 

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