TY - JOUR
T1 - Molecular cloning of cDNAs for two Xenopus proteasome subunits and their expression in adult tissues
AU - Fujii, Gen
AU - Tashiro, Kosuke
AU - Emori, Yasufumi
AU - Saigo, Kaoru
AU - Shiokawa, Koichiro
N1 - Funding Information:
We thank Prof. Koichi Suzuki and Dr. Hiroyuki Sorimachi (Institute of Applied Microbiology, University of Tokyo) for providing us with cDNA clones for rat proteasome subunits K and L. Also, we appreciate Miss Reiri Kurashima for her editing of the manuscript. This work was supported in part by grants from The Narishige Zoological Science Award (1991) and The Uehara Memorial Foundation (1992) to K.T.
PY - 1993/10/19
Y1 - 1993/10/19
N2 - Proteasome, a large protein complex with ATP-dependent protease activities, is composed of non-identical but closely related multi-subunits. Using cDNAs for rat proteasome subunits as probes, we obtained three cDNA clones for two Xenopus proteasome subunits from ovary cDNA library. The primary structures of the three cDNAs showed high homology to the corresponding proteasome subunits of other mammalian species (above 90%) and also considerable homology to those of Drosophila and yeast. These results indicate that the sequences of proteasome subunits are well conserved during evolution. Northern blot hybridization revealed that RNAs for the newly isolated subunits (XC8 and XC9) and the previously isolated subunit (XC3) occur at very high levels in testis and ovary, at moderately high levels in lung, skin kidney and spleen, and at low levels in liver, stomach and muscle. It was also shown that relative amounts of the mRNAs for the three subunits are similar in all the adult tissues examined. From these results, we concluded that the expression of the genes for the three subunits (XC3 XC8 and XC9-1) takes place in a roughly coordinated manner in different adult tissues.
AB - Proteasome, a large protein complex with ATP-dependent protease activities, is composed of non-identical but closely related multi-subunits. Using cDNAs for rat proteasome subunits as probes, we obtained three cDNA clones for two Xenopus proteasome subunits from ovary cDNA library. The primary structures of the three cDNAs showed high homology to the corresponding proteasome subunits of other mammalian species (above 90%) and also considerable homology to those of Drosophila and yeast. These results indicate that the sequences of proteasome subunits are well conserved during evolution. Northern blot hybridization revealed that RNAs for the newly isolated subunits (XC8 and XC9) and the previously isolated subunit (XC3) occur at very high levels in testis and ovary, at moderately high levels in lung, skin kidney and spleen, and at low levels in liver, stomach and muscle. It was also shown that relative amounts of the mRNAs for the three subunits are similar in all the adult tissues examined. From these results, we concluded that the expression of the genes for the three subunits (XC3 XC8 and XC9-1) takes place in a roughly coordinated manner in different adult tissues.
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U2 - 10.1016/0167-4781(93)90038-F
DO - 10.1016/0167-4781(93)90038-F
M3 - Article
C2 - 8218417
AN - SCOPUS:0027366355
SN - 0167-4781
VL - 1216
SP - 65
EP - 72
JO - Biochimica et Biophysica Acta - Gene Structure and Expression
JF - Biochimica et Biophysica Acta - Gene Structure and Expression
IS - 1
ER -