Rabouille C, Kuntz D A, Lockyer A, Watson R, Signorelli T, Rose D R, van den Heuvel M, Roberts D B
Genetics Unit, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
J Cell Sci. 1999 Oct;112 ( Pt 19):3319-30. doi: 10.1242/jcs.112.19.3319.
In this paper we show the organisation of the Drosophila gene encoding a Golgi alpha-mannosidase II. We demonstrate that it encodes a functional homologue of the mouse Golgi alpha-mannosidase II. The Drosophila and mouse cDNA sequences translate into amino acid sequences which show 41% identity and 61% similarity. Expression of the Drosophila GMII sequence in CHOP cells produces an enzyme which has mannosidase activity and is inhibited by swainsonine and by CuSO(4.) In cultured Drosophila cells and in Drosophila embryos, antibodies raised against a C-terminal peptide localise this product mainly to the Golgi apparatus as identified by cryo-immuno electron microscopy studies and by antibodies raised against known mammalian Golgi proteins. We discuss these results in terms of the possible use of dGMII as a Drosophila Golgi marker.
在本文中，我们展示了果蝇中编码高尔基体α-甘露糖苷酶II的基因的组织结构。我们证明它编码小鼠高尔基体α-甘露糖苷酶II的功能同源物。果蝇和小鼠的cDNA序列翻译成的氨基酸序列显示出41%的同一性和61%的相似性。果蝇GMII序列在CHOP细胞中的表达产生一种具有甘露糖苷酶活性的酶，该酶被苦马豆素和CuSO₄抑制。在培养的果蝇细胞和果蝇胚胎中，针对C末端肽产生的抗体将该产物主要定位到高尔基体，这是通过冷冻免疫电子显微镜研究以及针对已知哺乳动物高尔基体蛋白产生的抗体确定的。我们根据将dGMII用作果蝇高尔基体标记物的可能性来讨论这些结果。
