Beta-galactosidase activity in tissues of the plant parasite Cuscuta pentagona

Presenter Information

Ella LuceyFollow

Presenter Type

UNO Undergraduate Student

Major/Field of Study

Biology

Other

Molecular and Biomedical Biology

Advisor Information

(mschoenbeck@unomaha.edu) Mark Schoenbeck

Location

CEC RM #201/205/209

Presentation Type

Poster

Poster Size

36" X 24"

Start Date

22-3-2024 1:00 PM

End Date

22-3-2024 2:15 PM

Abstract

Beta-galactosidase (β-galactosidase) catalyzes the hydrolysis of a β-galactosidic bond, cleaving a galactose sugar from another organic moiety. β-galactosidase activities have been characterized in prokaryotic and eukaryotic organisms, mediating both metabolic and developmental processes. In plants, β-galactosidase activities are associated with cell wall modification. We have examined the distribution of β-galactosidase activity in the parasitic flowering plant Cuscuta pentagona through histological activity staining using the artificial substrate X-gal (5-bromo-4-chloro-3-indolyl-β-D-galactopyranoside). Abundant activity staining was observed in germinating seeds and seedlings, with the sites of highest activity varying as seedlings develop; this staining was pH sensitive, with the greater staining occurring under lower pH conditions. Activity staining was also observed in flowers, especially in the anthers. As a parasite, C. pentagona makes a penetrative structure, the haustorium, through which it extracts resources from its host plant. β-galactosidase activity was observed in these haustorial tissues. The cut ends of stem tissue segments were also observed to stain, while sites away from the cut did not. Experiments in which X-gal staining was observed at sites away from X-gal exposure suggest that activity at the cut site is a response to wounding, and not due to differential penetration of the stain.

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Mar 22nd, 1:00 PM Mar 22nd, 2:15 PM

Beta-galactosidase activity in tissues of the plant parasite Cuscuta pentagona

CEC RM #201/205/209

Beta-galactosidase (β-galactosidase) catalyzes the hydrolysis of a β-galactosidic bond, cleaving a galactose sugar from another organic moiety. β-galactosidase activities have been characterized in prokaryotic and eukaryotic organisms, mediating both metabolic and developmental processes. In plants, β-galactosidase activities are associated with cell wall modification. We have examined the distribution of β-galactosidase activity in the parasitic flowering plant Cuscuta pentagona through histological activity staining using the artificial substrate X-gal (5-bromo-4-chloro-3-indolyl-β-D-galactopyranoside). Abundant activity staining was observed in germinating seeds and seedlings, with the sites of highest activity varying as seedlings develop; this staining was pH sensitive, with the greater staining occurring under lower pH conditions. Activity staining was also observed in flowers, especially in the anthers. As a parasite, C. pentagona makes a penetrative structure, the haustorium, through which it extracts resources from its host plant. β-galactosidase activity was observed in these haustorial tissues. The cut ends of stem tissue segments were also observed to stain, while sites away from the cut did not. Experiments in which X-gal staining was observed at sites away from X-gal exposure suggest that activity at the cut site is a response to wounding, and not due to differential penetration of the stain.