Peroxisomal localization and function of NADP+ -specific isocitrate dehydrogenases in yeast.
Peroxisomal localization and function of NADP+ -specific isocitrate dehydrogenases in yeast.
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DOI：
10.1016/j.abb.2009.10.011
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发表时间：
2010-01-15
影响因子：
3.9
通讯作者：
McAlister-Henn L
中科院分区：
文献类型：
--
作者：
Lu Q;McAlister-Henn L
酵母过氧化物酶体NADP+特异性异柠檬酸脱氢酶（IDP 3）含有典型的I型过氧化物酶体靶向序列（羧基末端Cys-Lys-Leu三肽），并提供该细胞器中某些脂肪酸β-氧化所需的NADPH。携带PTS 1的胞质酵母IDP 2（IDP 2 +CKL）仅部分定位于过氧化物酶体，并且该酶能够代替过氧化物酶体IDP 3或胞质IDP 2发挥作用。类似的异柠檬酸脱氢酶（IDPA）从构巢曲霉，无论是否存在一个假定的PTS 1，被发现表现出模式的双房室分布和酵母中的双重功能类似于IDP 2 +CKL观察到的。为了测试过氧化物酶体水平的潜在细胞极限，过表达通常严格为过氧化物酶体的真酵母IDP 3。这也导致了双重分布和功能的酶在细胞质和过氧化物酶体，支持的可能性的限制细胞器量的IDP。
Yeast peroxisomal NADP+-specific isocitrate dehydrogenase (IDP3) contains a canonical type I peroxisomal targeting sequence (a carboxyl-terminal Cys-Lys-Leu tripeptide), and provides the NADPH required for β-oxidation of some fatty acids in that organelle. Cytosolic yeast IDP2 carrying a PTS1 (IDP2+CKL) was only partially localized to peroxisomes, and the enzyme was able to function in lieu of either peroxisomal IDP3 or cytosolic IDP2. The analogous isocitrate dehydrogenase enzyme (IDPA) from Aspergillus nidulans, irrespective of the presence or absence of a putative PTS1, was found to exhibit patterns of dual compartmental distribution and of dual function in yeast similar to those observed for IDP2+CKL. To test a potential cellular limit on peroxisomal levels, authentic yeast IDP3, which is normally strictly peroxisomal, was over-expressed. This also resulted in dual distribution and function of the enzyme in both the cytosol and in peroxisomes, supporting the possibility of a restriction on organellar amounts of IDP.
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影响因子：
3.9
作者：
Lu, Qian;Minard, Karyl I.;McAlister-Henn, Lee
通讯作者：
McAlister-Henn, Lee
影响因子：
4.8
作者：
Minard, KI;McAlister-Henn, L
通讯作者：
McAlister-Henn, L
影响因子：
2.8
作者：
Orij, Rick;Postmus, Jarne;Smits, Gertien J.
通讯作者：
Smits, Gertien J.
影响因子：
4.8
作者：
Geisbrecht, BV;Gould, SJ
通讯作者：
Gould, SJ
影响因子：
10.7
作者：
Nekrutenko, A;Hillis, DM;Baker, RJ
通讯作者：
Baker, RJ