ISSN 1392-3196 / e-ISSN 2335-8947
Zemdirbyste-Agriculture, vol. 106, No. 2 (2019), p. 183–190
Proteomic studies of honeybee- and manually-collected pollen
Veronika BORUTINSKAITĖ, Gražina TREIGYTĖ, Dalius MATUZEVIČIUS, Violeta ČEKSTERYTĖ, Bogumila KURTINAITIENĖ, Artūras SERACKIS, Dalius NAVAKAUSKAS,
In this study a new approach to quantitative and qualitative proteomic evaluation of pollen of different botanical origin was proposed. A monofloral mixture of plum (Prunus) – 86.83 ± 0.70% and willow (Salix spp.) – 13.7 ± 0.30% pollen, and monofloral plum (Prunus) pollen collected by bees was studied. Other pollen was collected manually from pear (Pyrus communis), apple tree (Malus sylvestris), cherry (Prunus / Cerasus) and wild cherry (Prunus avium). Samples were made during an early spring plant blossom. Proteins isolated from pollen samples were fractionated by a two-dimensional electrophoresis (2-DE) and about 50 proteins were identified using mass spectrometry analysis. A three-dimensional (3-D) visualization of proteins was performed. The intensities of protein spots differed in the orchard pollen samples more than ten times. The biological functions of the identified proteins differ, i.e. they are involved in transcription / translation, metabolic and other cellular processes.
The data revealed up-regulated process of the enzyme 5-methyltetrahydropteroyltriglutamate-homocysteine methyltransferase 1 in all pollen involved in methionine formation, which was the highest in monofloral orchard pollen collected by bees. This enzyme was identified in all the tested pollen. High level of expression of putative flavin-containing monooxygenase FMO GS-OX-like 11 protein was found in manually-collected pollen. This protein is important for plant protection against pathogens as well for plant hormone biosynthesis.
Key words: 2-D electrophoresis, 3-D visualization, mass spectrometry, pollen, proteins.
Full text: 106_2_str24.pdf