Chae S C, Maeda Y
Biological Institute, Graduate School of Science, Tohoku University, Sendai, Aoba, 980-77, Japan.
Biochem Biophys Res Commun. 1998 Apr 7;245(1):231-4. doi: 10.1006/bbrc.1998.8306.
A proteasome subunit-1 gene (DAPS-1) was isolated as one preferentially expressed during the transition from growth to differentiation in Dictyostelium discoideum cells, using the differential display method. The DAPS-1 cDNA sequence with a length of 882 bp encodes a protein (Mr. 23.4 kDa) consisting of 213 amino acids. The deduced amino acid sequence of DAPS-1 showed 61% and 58% identity to the proteasome subunit Y of Xenopus laevis and Homo sapiens, respectively and 48% and 47% identity to the proteasome subunit LMP2 of Homo sapiens and Orizas latipes, respectively. Northern analysis revealed that a 1.0 kb of DAPS-1 mRNA is predominantly expressed during the early stage of differentiation induced by starvation. This seems to indicate that the DAPS-1 protein may be involved in proteolysis coupled with active exchange of the cellular protein composition during the phase-shift of Dictyostelium cells from the proliferative to differentiated state.
利用差异显示法，分离出一种蛋白酶体亚基1基因（DAPS - 1），它是在盘基网柄菌细胞从生长向分化转变过程中优先表达的基因。长度为882 bp的DAPS - 1 cDNA序列编码一个由213个氨基酸组成的蛋白质（分子量23.4 kDa）。推导的DAPS - 1氨基酸序列与非洲爪蟾和人类的蛋白酶体亚基Y分别有61%和58%的同一性，与人类和日本青鳉的蛋白酶体亚基LMP2分别有48%和47%的同一性。Northern分析显示，在饥饿诱导的分化早期，1.0 kb的DAPS - 1 mRNA大量表达。这似乎表明，DAPS - 1蛋白可能在盘基网柄菌细胞从增殖状态向分化状态转变过程中，参与了与细胞蛋白质组成的活跃交换相关的蛋白水解作用。
