Dehydrin stress proteins in Pinus sylvestris L. needles under conditions of extreme climate of Yakutia.

This is the first study to investigate stress proteins dehydrins with the use of specific antibodies in the Scots pine (Pinus sylvestris L.) needles and their changes in the annual cycle under extreme climate of Yakutia. No pronounced polymorphism of major dehydrins (14-15 and 66 kDa) has been found during the winter dormancy period of P. sylvestris. A clear correlation between the seasonal variations in dehydrins and changes in the water content in needles was revealed. Consistently high levels of dehydrins was retained throughout the period of low negative temperatures. It is assumed that dehydrins can participate in the formation of P. sylvestris L. resistance to the permafrost conditions.

DEHYDRIN- STRESS PROTEINS OF BIRCH BUDS IN CONTRASTING CLIMATIC REGIONS.

Stress proteins dehydrins have been identified using specific antibodies in buds silver birch (Betula pendula Roth) growing in contrasting climatic conditions of the regions Karelia and Central Yakutia. Dehydrins in buds of plants are presented in two areas: medium molecular weight (56-73 kDa) and low molecular weight (14-21 kDa), and 17 kDa dehydrin was detected in all studied birches. 14-21 kDa dehydrins are the most susceptible to seasonal changes. Regardless of birch growing region, dehydrines 14-21 kDa show significant increase in their level in the autumn and winter when the trees are characterized by the highest frost resistances. Dehydrins have relealed intraspecific polymorphism, more pronounced in Yakutia plants in conditions of extreme continental climate, compared with Karelia, which is probably due to the peculiarities of woody plants to adapt to the extremely low winter temperature of the permafrost zone.

[Characterization of aldehyde dehydrogenase gene fragment from mung bean Vigna radiata using the polymerase chain reaction]. / Kharakteristika fragmenta gena al'degiddegidrogenazy mash Vigna radiata s pomoshch'iu metoda polimeraznoi tsepnoi reaktsii.

Two degenerate oligonucleotide sequence primers and polymerase chain reactions on total DNA have been utilized to clone on 651--bp gene fragment coding the central part of amino acid sequence of an earlier unknown aldehyde dehydrogenase (ALDH) from mung bean. The deduced partial amino acid sequence for this aldehyde dehydrogenase shows about 65% sequence identity to ALDHs of Vibrio cholerae Rhodococcus sp., Alcaligenes eutrophus and about 45% sequence identity to mammalian ALDHs 1 and 2, ALDHs of Aspergillus niger and A, nidulans, the betain aldehyde dehydrogenase from spinach. Alignment of the mung bean aldehyde dehydrogenase partial amino acid sequence with the sequence of 16 NAD(P)(+)-dependent aldehyde dehydrogenases has demonstrated that all strictly conserved amino acid residues and all three conservative regions are identical.