Dehydrogenase Activities of the Pentose Phosphate Pathway in Tobacco Leaf Epidermis infected with Tobacco Mosaic Virus

Takahashi, Tsuyoshi

doi:10.1111/j.1439-0434.1971.tb03177.x

Cited by 9 publications

(1 citation statement)

References 7 publications

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“…The observations about the influence of viral infection on the rate of the oxidative pentose phosphate pathway do not correspond with one another; some authors have reported a decreased rate (Bozart 1969), others an unchanged rate (Takahashi 1971), but most research workers have found increased activities of the enzymes involved in the pathway (especially of the two dehydrogenases) in tissues predominantly surrounding local necrotic lesions (Solymosy and Farkas 1962;Simons and Ross 1971;Huth 1973 and others). The results obtained in our earlier studies also confirmed the stimulation of the oxidative pentose phosphate pathway (Sˇindela´rˇ1986; Sˇindela´rˇand Sˇindela´rˇova´1987a, b;Sˇindela´rˇet al 1990Sˇindela´rˇet al , 1999Sˇindela´rˇova´et al 1997Sˇindela´rˇova´et al , 1998.…”

Section: Introductionmentioning

confidence: 93%

Correlation of viral RNA biosynthesis with glucose-6-phosphate dehydrogenase activity and host resistance

Šindelář

Šindelářová

2002

Planta

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Changes in glucose-6-phosphate dehydrogenase (G6P DH; EC 1.1.1.49) activity caused by infection of tobacco ( Nicotiana tabacum L.) leaves with potato virus Y (PVY), cucumber mosaic virus, potato virus X, tobacco rattle virus and turnip mosaic virus, the subcellular localisation of G6P DH isozymes in mesophyll protoplasts derived from healthy and PVY-infected tobacco leaves, as well as G6P DH control and the relationship of its isozymes with the degree of tobacco resistance to PVY multiplication, were studied. The activities of G6P DH were markedly increased in locally and systemically infected leaves and the time courses of the activity linearly correlated with those of virus multiplication. In leaves infected with PVY, the activity time courses of the crude and the partially purified G6P DH were coincident. This probably indicates the involvement of coarse regulation of the enzyme. PVY content linearly correlated with enhanced G6P DH activity in leaf discs derived from susceptible, tolerant and resistant cultivars of tobacco. The increased activity of the enzyme in infected protoplasts and plant tissues was predominantly caused by the increased activity of chloroplastic isozymes. This was confirmed by the specific staining of isozymes after electrophoretic separation of chloroplastic proteins of tobacco leaves. These findings enable the degree of resistance to virus multiplication to be quantified for the use of gene manipulation and breeding.

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Section: Introductionmentioning

confidence: 93%