NDLI: Expression of different forms of transglutaminases by immature cells of Helianthus tuberosus sprout apices

Content Provider	Springer Nature Link
Author	Beninati, Simone Iorio, Rosa Anna Tasco, Gianluca Serafini Fracassini, Donatella Casadio, Rita Del Duca, Stefa
Copyright Year	2012
Abstract	Immature cells of etiolated apices of sprouts growing from Helianthus tuberosus (H. t.) tubers showed Ca2+-dependent transglutaminase (TG, EC 2.3.2.13) activity on fibronectin (more efficiently) and dimethylcasein as substrates. Three main TG bands of about 85, 75 and 58 kDa were isolated from the 100,000×g apices supernatant through a DEAE-cellulose column at increasing NaCl concentrations and immuno-identified by anti-TG K and anti-rat prostate gland TG antibodies. These three fractions had catalytic activity as catalyzed polyamine conjugation to N-benzyloxycarbonyl-L-γ-glutaminyl-L-leucine (Z-L-Gln-L-Leu) and the corresponding glutamyl-derivatives were identified. The amino acid composition of these TG proteins was compared with those of several sequenced TGs of different origin. The composition of the two larger bands presented great similarities with annotated TGs; in particular, the 75 kDa form was very similar to mammalian inactive EPB42. The 58 kDa form shared a low similarity with other TGs, including a maize sequence of similar molecular mass, which, however, did not present the catalytic triad in the position of all annotated TGs. A 3D model of the H. t. TGs was built adopting TG2 as template. These novel plant TGs are hypothesized to be constitutive and discussed in relation to their possible roles in immature cells. These data suggest that in plants, multiple TG forms are active in the same organ and that plant and animal enzymes probably are very close not only for their catalytic activity but also structurally.
Starting Page	271
Ending Page	283
Page Count	13
File Format	PDF
ISSN	09394451
Journal	Amino Acids
Volume Number	44
Issue Number	1
e-ISSN	14382199
Language	English
Publisher	Springer Vienna
Publisher Date	2012-10-18
Publisher Place	Vienna
Access Restriction	Subscribed
Subject Keyword	Plant transglutaminases (γ-Glutamyl)-polyamines Spermidine Post-translational modification Helianthus tuberosus Meristems Biochemistry Analytical Chemistry Biochemical Engineering Life Sciences Proteomics Neurobiology
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Biochemistry Clinical Biochemistry

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