Importance of cytomatrix-bound polysomes to synthesis of lysine-containing proteins in triticale germs under ABA treatment

• Autorzy: Szypulska E. , Weidner S.
• Języki publikacji: EN

Abstrakty

EN

The influence of exogenous abscisic acid (ABA) on the content of free polysomes (FP), membranebound polysomes (MBP), cytoskeleton-bound polysomes (CBP) and cytomatrix-bound polysomes (CMBP) in triticale germs as well as in vitro protein synthesis by these four polysomal fractions were studied. During translation, proteins were biotinylated for chemiluminescence detection. We have found that ABA changed both the content of FP, MBP, CMP and CMBP in germ tissue, and their subsequent translation activity. At 100 µM ABA, the content of FP and MBP was over fourfold lower compared to the control, whereas the amounts of CBP and CMBP were about two- and threefold higher, respectively. Moreover, the estimation of the share of polysomes in each ribosomal fraction (sub-units, monosomes, polysomes) showed that, at 100 µM ABA, cytomatrix-bound polysomes, which constituted 90% of polysomes, were the predominant class in ABA-treated germs while membrane-bound polysomes, which made up 82% of polysomes, dominated in the control. A high level of CMBP in ABA-treated tissues may indicate that this class of polysomes participates in ABAinduced synthesis of proteins. In turn, the inhibition of MBP under ABA-treatment is probably due to the delayed protein synthesis which takes place on these polysomes. We identified two lysine-containing proteins synthesized on both of the above classes of polysomes, whose synthesis was altered due to ABA application. Synthesis of a 47 kDa protein on MBP was inhibited, while synthesis of a 79 kDa protein on CMBP is strongly enhanced by ABA influence. The importance of these findings is discussed.

• Wydawca: -
• Czasopismo: Acta Physiologiae Plantarum
• Rocznik: 2011
• Tom: 33
• Numer: 4
• Opis fizyczny: p.1461-1465,fig.,ref.

Twórcy

autor

Szypulska E.

• Department of Biochemistry, Faculty of Biology, University of Warmia and Mazury in Olsztyn, M. Oczapowskiego St., 1A, 10-957, Olsztyn-Kortowo, Poland

autor

Weidner S.

• Department of Biochemistry, Faculty of Biology, University of Warmia and Mazury in Olsztyn, M. Oczapowskiego St., 1A, 10-957, Olsztyn-Kortowo, Poland

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