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Molecular characterization of a fourth isoform of the catalytic subunit of protein phosphatase 2A fromArabidopsis thaliana

✍ Scribed by Antonio Casamayor; Encarna Pérez-Callejón; Gemma Pujol; Joaquín Ariño; Albert Ferrer


Publisher
Springer
Year
1994
Tongue
English
Weight
582 KB
Volume
26
Category
Article
ISSN
0167-4412

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✦ Synopsis


We have recently reported the existence of multiple isoforms of the catalytic subunit of protein phosphatase 2A (PP2A) in Arabidopsis thaliana and the molecular cloning of cDNAs encoding three of these proteins (PP2A-1, PP2A-2, PP2A-3). The reported cDNA encoding PP2A-3 was truncated at the 5' terminus, lacking a short fragment of the N-terminal coding sequence. We have now isolated a near full-length cDNA encoding the entire PP2A-3 protein (313 residues). The clone includes 188 nucleotides of 5'-untranslated region, where a 44 bp long poly(GA) track is found. We also describe the cloning of a cDNA encoding a fourth isoform of PP2A (PP2A-4). The polypeptide contains 313 residues being 98 ~o identical to PP2A-3 and only 80~o identical to both PP2A-1 and PP2A-2. The mRNA for PP2A-4 is 1.4 kb in length and, although predominantly expressed in roots, it is also found in other organs. It is concluded that in A. thaliana the isoforms of PP2A can be grouped in two extremely conserved subfamilies.


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Crystallization of the Aα subunit of pro
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## Abstract The Aα subunit of human protein phosphatase 2A forms crystals in space group __P__2~1~ with cell dimensions __a__ = 104.0, __b__ = 174.9, c = 168.2 Å, and β angle = 90.2°. At cryogenic temperatures, the crystals diffracted to a resolution limit of ∼ 3.0 Å. Based on the unit cell dimensi