Cloning and sequence analysis of a full-length cDNA of SmPP1cb encoding turbot protein phosphatase 1 beta catalytic subunit

Fei Qi; Huarong Guo; Jian Wang

doi:10.1007/s00343-008-0054-z

Your Location：

Home >

Browse articles >

Cloning and sequence analysis of a full-length cDNA of SmPP1cb encoding turbot protein phosphatase 1 beta catalytic subunit

Updated：2023-05-16

- Cloning and sequence analysis of a full-length cDNA of SmPP1cb encoding turbot protein phosphatase 1 beta catalytic subunit
- Journal of Oceanology and Limnology Vol. 26, Issue 1, Pages: 54-61(2008)
- Affiliations：
  
  Ocean University of China
- Author bio：
- Funds：
- DOI：10.1007/s00343-008-0054-z
  CLC：
- Published：2008
- Accepted：
Scan QR Code
Qi, F., Guo, H. & Wang, J. Cloning and sequence analysis of a full-length cDNA of SmPP1cb encoding turbot protein phosphatase 1 beta catalytic subunit., Chin. J. Ocean. Limnol. 26, 54–61 (2008). https://doi.org/10.1007/s00343-008-0054-z
DOI：

Qi, F., Guo, H. & Wang, J. Cloning and sequence analysis of a full-length cDNA of SmPP1cb encoding turbot protein phosphatase 1 beta catalytic subunit., Chin. J. Ocean. Limnol. 26, 54–61 (2008). https://doi.org/10.1007/s00343-008-0054-z DOI：

摘要

Abstract

Reversible protein phosphorylation

catalyzed by protein kinases and phosphatases

is an important and versatile mechanism by which eukaryotic cells regulate almost all the signaling processes. Protein phosphatase 1 (PP1) is the first and well-characterized member of the protein serine/threonine phosphatase family. In the present study

a full-length cDNA encoding the beta isoform of the catalytic subunit of protein phosphatase 1(PP1cb)

was for the first time isolated and sequenced from the skin tissue of flatfish turbot Scophthalmus maximus

designated SmPP1cb

by the rapid amplification of cDNA ends (RACE) technique. The cDNA sequence of SmPP1cb we obtained contains a 984 bp open reading frame (ORF)

flanked by a complete 39 bp 5′ untranslated region and 462 bp 3′ untranslated region. The ORF encodes a putative 327 amino acid protein

and the N-terminal section of this protein is highly acidic

Met-Ala-Glu-Gly-Glu-Leu-Asp-Val-Asp

a common feature for PP1 catalytic subunit but absent in protein phosphatase 2B (PP2B). And its calculated molecular mass is 37 193 Da and pI 5.8. Sequence analysis indicated that

SmPP1cb is extremely conserved in both amino acid and nucleotide acid levels compared with the PP1cb of other vertebrates and invertebrates

and its Kozak motif contained in the 5′UTR around ATG start codon is GXXAXXGXXATGG

which is different from mammalian in two positions A−6 and G−3

indicating the possibility of different initiation of translation in turbot

and also the 3′UTR of SmPP1cb is highly diverse in the sequence similarity and length compared with other animals

especially zebrafish. The cloning and sequencing of SmPP1cb gene lays a good foundation for the future work on the biological functions of PP1 in the flatfish turbot.

关键词

Keywords

references

Aerne, B. and D. Ish-Horowicz, 2004. Receptor tyrosine phosphatase y is required for Delta/Notch signaling and cyclic gene expression in the presomitic mesoderm. Development 131: 3 391–3 399.

Barford, D., 1995. Protein phosphatases. Curr. Opin. Struct. Biol. 5(6): 728–734.

Barker, H. M., N. D. Brewis, A. J. Street, N. K. Spurr and P. T. W. Cohen, 1994. Three genes for protein phosphatase 1 map to different human chromosomes: sequence, expression and gene localization of protein serine/threonine phosphatase 1 beta (PPP1cb). Biochim. Biophys. Acta 1220: 212–218.

Booher, R. and D. Beach, 1989. Involvement of a type 1 protein phosphatase encoded by bws1 + in fission yeast mitotic control. Cell 57: 1 009–1 016.

Brautigan, D. L., 1995. Flicking the switches: phosphorylation of serine/threonine protein phosphatases. Seminars in Cancer Biology 6: 211–217.

Cohen, P. T. W., 1997. Novel protein serine/threonine phosphatases: variety is the spice of life. Trends. Biochem. Sci. 22: 245–251.

Conde, R., J. Xavier, C. McLoughlin, M. Chinkers and N. Ovsenek, 2005. Protein phosphatase 5 is a negative modulator of heat shock factor 1. J. Biol. Chem. 280(32): 28 989–28 996.

Davuluri, R. V., Y. Suzuki, S. Sugano and M. Q. Zhang, 2000. CART Classification of Human 5′ UTR Sequences. Genome Res. 10: 1 807–1 816.

Dombrádi, V., D. J. Mann, R. D. Saunders and P. T. W. Cohen, 1993. Cloning of the fourth functional gene for protein phosphatase 1 in Drosophila melanogaster from its chromosomal location. Eur. J. Biochem. 212: 177–183.

Gallego, M. and D. M. Virshup, 2005. Protein serine/threonine phosphatases: life, death, and sleeping. Curr. Opin. Cell Biol. 17: 197–202.

Goldberg, J., H. Huang, Y. Kwon, P. Greengard, A. C. Nairn and J. Kuriyan, 1995. Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1. Nature 376: 745–753.

Higgins, D. G., A. J. Bleasby and R. Fuchs, 1992. Clustal V: improved software for multiple sequence alignment. Comput. Appl. Biosci. 8: 189–191.

Hunter, T., 1995. Protein kinase and phosphatases: the Yin and Yang of protein phosphorylation and signaling. Cell 80: 225–236.

Kozak, M., 1981. Possible role of flanking nucleotides in recognition of the AUG initiator codon by eukaryotic ribosomes. Nucleic Acids Research 9(20): 5 233–5 252.

Kozak, M., 1986. Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes. Cell 44(2): 283–292.

Kozak, M., 1987. An analysis of 5′-noncoding sequences from 699 vertebrate messenger RNAs. Nucleic Acids Research 15(20): 8 125–8 148.

Kozak, M., 1991. Structural features in eukaryotic mRNAs that modulate the initiation of translation. J. Biol. Chem. 266: 19 867–19 870.

Lin, Q., E. S. Buckler IV, S. V. Muse and J. C. Walker, 1999. Molecular evolution of type 1 serine/threonine protein phosphatases. Molecular Phylogenetics and Evolution 12(1): 57–66.

Menzel, D., O. Vugrek, S. Frank and C. Elsner-Menzel, 1995. Protein phosphatase 2A, a potential regulator of actin dynamics and actin-based organelle motility in the green alga Acetabularia. Eur. J. Cell Biol. 67(2): 179–187.

Pondaven, P. and P. Cohen, 1987. Identification of protein phosphatases-1 and 2A and inhibitor-2 in oocytes of the starfish Asterias rubens and Marthasterias glacialis. Eur. J. Biochem. 167(1): 135–140.

Saitou, N. and M. Nei, 1987. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 4: 406–425.

Sar, A. M. V. D., J. D. Fockert, M. Betist, D. Zivkovic and J. D. Hertog, 1999. Pleiotropic effects of zebrafish Protein-Tyrosine Phosphatase-1B on early embryonic development. Int. J. Dev. Biol. 43: 785–794.

Sasaki, K., H. Shima, Y. Kitagawa, S. Irino, T. Sugimura and M. Nagao, 1990. Identification of members of the protein phosphatase 1 gene family in the rat and enhanced expression of protein phosphatase1 v-alpha gene in rat hepatocellular carcinomas. Jpn. J. Cancer Res. 81: 1 272–1 280.

Smith, R. D., Q. Lin, J. F. Cannon and J. C. Walker, 1995. Type-1 and type-2C protein phosphatases of higher plants. Adv. Protein Phosphatases 9: 105–120.

Watanabe, T., H. B. Huang, A. Horiuchi, E. F. da Cruze Silva, L. Hsieh-Wilson, P. B. Allen, S. Shenolikar, P. Greengard and A. C. Nairn, 2001. Protein phosphatase 1 regulation by inhibitors and targeting subunits. Proc. Natl. Acad. Sci. USA 98: 3 080–3 085.

Wozniak, E., S. Oldziej and J. Ciarkowski, 2000. Molecular modeling of the catalytic domain of serine/threonine phosphatase-1 with the Zn2+ and Mn2+ di-nuclear ion centers in the active site. Computers and Chemistry 24: 381–390.

Zeke, T., P. Gergely and V. Dombrádi, 1998. The catalytic subunits of Ser/Thr protein phosphatases from Caenorhabditis elegans. Comp. Biochem. Physiol. 119B(2): 317–324.

Views

Downloads

CSCD

Alert me when the article has been cited

Submit

Tools

Publicity Resources

Morphological comparison and gonadotropins cell localization of mature female turbot and mouse pituitary

The ontogeny of acidic digestive tract in larval turbot Scophthalmus maximus based on H⁺/K⁺-ATPase and pepsinogen

Impact assessment of modified clay on embryo-larval stages of turbot Scophthalmus maximus L.

Characterization and differential expression of three GnRH forms during reproductive development in cultured turbot Schophthalmus maximus

PI Gain Scheduling Control for Flight EnvironmentSimulation System of Altitude Ground TestFacilities Based on LMI Pole Assignment

Related Author

Jinxing LIN

Yunhong GAO

Yudong JIA

Liang CHI

Jun LI

Daoyuan MA

Zhizhong XIAO

Qinghua LIU

Related Institution

Shanghai Laboratory Animal Research Center

Yellow Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences

Conson Oriental (Yantai) Recirculating Aquaculture Technology Co., Ltd.

Southern Marine Science and Engineering Guangdong Laboratory

Laboratory for Marine Biology and Biotechnology, Pilot National Laboratory for Marine Science and Technology

Address：Editorial Office of JOL, 88 Haijun Rd. Qingdao, 266000, China
Tel：+86-532-82898754 Email：jol@qdio.ac.cn
Technical support is provided by Beijing Founder electronics co., LTD 京ICP备09064830号-19 京公网安备11010802024621
It is recommended to read the content of this site in Chrome&IE9+. Please switch to extreme mode in browser 360.
Cookies We use cookies to help provide and enhance our service and tailor content. By continuing, you agree to the use of cookies.

⁰