Molecular cloning and developmental expression of the catalytic and 65-kDa regulatory subunits of protein phosphatase 2A in Drosophila
Mayer-Jaekel, Regina E. ; Baumgartner, Stefan LU
; Bilbe, Graeme
; Ohkura, Hiroyuki
; Glover, David M.
and Hemmings, Brian A.
(1992)
In Molecular Biology of the Cell
3(3).
p.287-298
- Abstract
cDNA clones encoding the catalytic subunit and the 65-kDa regulatory subunit of protein phosphatase 2A (PR65) from Drosophila melanogaster have been isolated by homology screening with the corresponding human cDNAs. The Drosophila clones were used to analyze the spatial and temporal expression of the transcripts encoding these two proteins. The Drosophila PR65 cDNA clones contained an open reading frame of 1773 nucleotides encoding a protein of 65.5 kDa. The predicted amino acid sequence showed 75 and 71% identity to the human PR65 α and β isoforms, respectively. As previously reported for the mammalian PR65 isoforms, Drosophila PR65 is composed of 15 imperfect repeating units of ∼39 amino acids. The residues contributing to this repeat... (More)
cDNA clones encoding the catalytic subunit and the 65-kDa regulatory subunit of protein phosphatase 2A (PR65) from Drosophila melanogaster have been isolated by homology screening with the corresponding human cDNAs. The Drosophila clones were used to analyze the spatial and temporal expression of the transcripts encoding these two proteins. The Drosophila PR65 cDNA clones contained an open reading frame of 1773 nucleotides encoding a protein of 65.5 kDa. The predicted amino acid sequence showed 75 and 71% identity to the human PR65 α and β isoforms, respectively. As previously reported for the mammalian PR65 isoforms, Drosophila PR65 is composed of 15 imperfect repeating units of ∼39 amino acids. The residues contributing to this repeat structure show also the highest sequence conservation between species, indicating a functional importance for these repeats. The gene encoding Drosophila PR65 was located at 29B1,2 on the second chromosome. A major transcript of 2.8 kilobase (kb) encoding the PR65 subunit and two transcripts of 1.6 and 2.5 kb encoding the catalytic subunit could be detected throughout Drosophila development. All of these mRNAs were most abundant during early embryogenesis and were expressed at lower levels in larvae and adult flies. In situ hybridization of different developmental stages showed a colocalization of the PR65 and catalytic subunit transcripts. The mRNA expression is high in the nurse cells and oocytes, consistent with a high equally distributed expression in early embryos. In later embryonal development, the expression remains high in the nervous system and the gonads but the overall transcript levels decrease. In third instar larvae, high levels of mRNA could be observed in brain, imaginai discs, and in salivary glands. These results indicate that protein phosphatase 2A transcript levels change during development in a tissue and in a time-specific manner.
(Less)
- author
- Mayer-Jaekel, Regina E.
; Baumgartner, Stefan
LU
; Bilbe, Graeme
; Ohkura, Hiroyuki
; Glover, David M.
and Hemmings, Brian A.
- publishing date
- 1992-01-01
- type
- Contribution to journal
- publication status
- published
- in
- Molecular Biology of the Cell
- volume
- 3
- issue
- 3
- pages
- 287 - 298
- publisher
- American Society for Cell Biology
- external identifiers
-
- scopus:0027055504
- pmid:1320961
- ISSN
- 1059-1524
- DOI
- 10.1091/mbc.3.3.287
- language
- English
- LU publication?
- no
- id
- aa46cb24-2ee2-44cc-aeb8-20ebf96ddf98
- date added to LUP
- 2019-05-21 14:10:09
- date last changed
- 2024-01-01 05:55:34
@article{aa46cb24-2ee2-44cc-aeb8-20ebf96ddf98,
abstract = {{<p>cDNA clones encoding the catalytic subunit and the 65-kDa regulatory subunit of protein phosphatase 2A (PR65) from Drosophila melanogaster have been isolated by homology screening with the corresponding human cDNAs. The Drosophila clones were used to analyze the spatial and temporal expression of the transcripts encoding these two proteins. The Drosophila PR65 cDNA clones contained an open reading frame of 1773 nucleotides encoding a protein of 65.5 kDa. The predicted amino acid sequence showed 75 and 71% identity to the human PR65 α and β isoforms, respectively. As previously reported for the mammalian PR65 isoforms, Drosophila PR65 is composed of 15 imperfect repeating units of ∼39 amino acids. The residues contributing to this repeat structure show also the highest sequence conservation between species, indicating a functional importance for these repeats. The gene encoding Drosophila PR65 was located at 29B1,2 on the second chromosome. A major transcript of 2.8 kilobase (kb) encoding the PR65 subunit and two transcripts of 1.6 and 2.5 kb encoding the catalytic subunit could be detected throughout Drosophila development. All of these mRNAs were most abundant during early embryogenesis and were expressed at lower levels in larvae and adult flies. In situ hybridization of different developmental stages showed a colocalization of the PR65 and catalytic subunit transcripts. The mRNA expression is high in the nurse cells and oocytes, consistent with a high equally distributed expression in early embryos. In later embryonal development, the expression remains high in the nervous system and the gonads but the overall transcript levels decrease. In third instar larvae, high levels of mRNA could be observed in brain, imaginai discs, and in salivary glands. These results indicate that protein phosphatase 2A transcript levels change during development in a tissue and in a time-specific manner.</p>}},
author = {{Mayer-Jaekel, Regina E. and Baumgartner, Stefan and Bilbe, Graeme and Ohkura, Hiroyuki and Glover, David M. and Hemmings, Brian A.}},
issn = {{1059-1524}},
language = {{eng}},
month = {{01}},
number = {{3}},
pages = {{287--298}},
publisher = {{American Society for Cell Biology}},
series = {{Molecular Biology of the Cell}},
title = {{Molecular cloning and developmental expression of the catalytic and 65-kDa regulatory subunits of protein phosphatase 2A in Drosophila}},
url = {{http://dx.doi.org/10.1091/mbc.3.3.287}},
doi = {{10.1091/mbc.3.3.287}},
volume = {{3}},
year = {{1992}},
}