TY - JOUR
T1 - Molecular cloning of a novel isotype of Mg2+-dependent protein phosphatase β (type-2Cβ) enriched in brain and heart
AU - Terasawa, Takayuki
AU - Kobayashi, Takayasu
AU - Murakami, Takashi
AU - Ohnishi, Motoko
AU - Kato, Shunsuke
AU - Tanaka, Osamu
AU - Kondo, Hisatake
AU - Yamamoto, Hiroaki
AU - Takeuchi, Takuji
AU - Tamura, Shinri
PY - 1993/1/1
Y1 - 1993/1/1
N2 - Two complementary DNA (cDNA) clones (pTK- 1 and-2) encoding two distinct isotypes of mouse Mg2+-dependent protein phosphatase β (MPPβ-1 and -2, respectively) were isolated from a melanocyte cDNA library. Although mouse pTK-1 is orthologous to the rat cDNA (JW5) reported previously [Wenk, J., Trompeter, H. I., Pettrich, K. G., Cohen, P. T. W., Campbell, D. G., and Mieskes, G. (1992) FEBS Lett. 297, 135-138], pTK-2 is a novel cDNA clone. It was strongly suggested that the pTK-1 and -2 cDNAs are splicing variants of a single pre-mRNA. The difference in the amino acid sequences between MPPβ-1 and -2 was observed only at the carboxyterminal regions. Both the recombinant MPPβ-1 and -2 expressed in Escherichia coli cells were immunoreactive to an anti-MPPβ antibody and exhibited Mg2+-dependent and okadaic acid-insensitive protein phosphatase activities with similar substrate specificities. Although the mRNA of MPPβ-1 was expressed ubiquitously in various mouse tissues, that of MPPβ-2 was expressed exclusively in brain and heart. These results suggest the difference in the physiological roles of these two enzyme isotypes.
AB - Two complementary DNA (cDNA) clones (pTK- 1 and-2) encoding two distinct isotypes of mouse Mg2+-dependent protein phosphatase β (MPPβ-1 and -2, respectively) were isolated from a melanocyte cDNA library. Although mouse pTK-1 is orthologous to the rat cDNA (JW5) reported previously [Wenk, J., Trompeter, H. I., Pettrich, K. G., Cohen, P. T. W., Campbell, D. G., and Mieskes, G. (1992) FEBS Lett. 297, 135-138], pTK-2 is a novel cDNA clone. It was strongly suggested that the pTK-1 and -2 cDNAs are splicing variants of a single pre-mRNA. The difference in the amino acid sequences between MPPβ-1 and -2 was observed only at the carboxyterminal regions. Both the recombinant MPPβ-1 and -2 expressed in Escherichia coli cells were immunoreactive to an anti-MPPβ antibody and exhibited Mg2+-dependent and okadaic acid-insensitive protein phosphatase activities with similar substrate specificities. Although the mRNA of MPPβ-1 was expressed ubiquitously in various mouse tissues, that of MPPβ-2 was expressed exclusively in brain and heart. These results suggest the difference in the physiological roles of these two enzyme isotypes.
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U2 - 10.1006/abbi.1993.1598
DO - 10.1006/abbi.1993.1598
M3 - Article
C2 - 8274020
AN - SCOPUS:0027131224
VL - 307
SP - 342
EP - 349
JO - Archives of Biochemistry and Biophysics
JF - Archives of Biochemistry and Biophysics
SN - 0003-9861
IS - 2
ER -