Wojtas K, Slepecky N, von Kalm L, Sullivan D
Department of Biology, Syracuse University, New York 13244, USA.
Mol Biol Cell. 1997 Sep;8(9):1665-75. doi: 10.1091/mbc.8.9.1665.
Structural relationships between the myofibrillar contractile apparatus and the enzymes that generate ATP for muscle contraction are not well understood. We explored whether glycolytic enzymes are localized in Drosophila flight muscle and whether localization is required for function. We find that glycerol-3-phosphate dehydrogenase (GPDH) is localized at Z-discs and M-lines. The glycolytic enzymes aldolase and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) are also localized along the sarcomere with a periodic pattern that is indistinguishable from that of GPDH localization. Furthermore, localization of aldolase and GAPDH requires simultaneous localization of GPDH, because aldolase and GAPDH are not localized along the sarcomere in muscles of strains that carry Gpdh null alleles. In an attempt to understand the process of glycolytic enzyme colocalization, we have explored in more detail the mechanism of GPDH localization. In flight muscle, there is only one GPDH isoform, GPDH-1, which is distinguished from isoforms found in other tissues by having three C-terminal amino acids: glutamine, asparagine, and leucine. Transgenic flies that can produce only GPDH-1 display enzyme colocalization similar to wild-type flies. However, transgenic flies that synthesize only GPDH-3, lacking the C-terminal tripeptide, do not show the periodic banding pattern of localization at Z-discs and M-lines for GPDH. In addition, neither GAPDH nor aldolase colocalize at Z-discs and M-lines in the sarcomeres of muscles from GPDH-3 transgenic flies. Failure of the glycolytic enzymes to colocalize in the sarcomere results in the inability to fly, even though the full complement of active glycolytic enzymes is present in flight muscles. Therefore, the presence of active enzymes in the cell is not sufficient for muscle function; colocalization of the enzymes is required. These results indicate that the mechanisms by which ATP is supplied to the myosin ATPase, for muscle contraction, requires a highly organized cellular system.
肌原纤维收缩装置与为肌肉收缩产生ATP的酶之间的结构关系尚未完全清楚。我们探究了糖酵解酶是否定位于果蝇飞行肌中,以及定位对于其功能是否是必需的。我们发现甘油-3-磷酸脱氢酶(GPDH)定位于Z线和M线。糖酵解酶醛缩酶和甘油醛-3-磷酸脱氢酶(GAPDH)也沿肌节呈周期性分布,其模式与GPDH的定位难以区分。此外,醛缩酶和GAPDH的定位需要GPDH同时定位,因为在携带Gpdh无效等位基因的品系的肌肉中,醛缩酶和GAPDH不沿肌节定位。为了试图理解糖酵解酶共定位的过程,我们更详细地探究了GPDH定位的机制。在飞行肌中,只有一种GPDH同工型,即GPDH-1,它与在其他组织中发现的同工型的区别在于有三个C端氨基酸:谷氨酰胺、天冬酰胺和亮氨酸。只能产生GPDH-1的转基因果蝇表现出与野生型果蝇相似的酶共定位。然而,只合成缺少C端三肽的GPDH-3的转基因果蝇,在Z线和M线处未显示出GPDH定位的周期性条带模式。此外,在GPDH-3转基因果蝇肌肉的肌节中,GAPDH和醛缩酶在Z线和M线处均未共定位。即使飞行肌中存在完整的活性糖酵解酶,但糖酵解酶在肌节中不能共定位导致无法飞行。因此,细胞中存在活性酶对于肌肉功能是不够的;酶的共定位是必需的。这些结果表明,为肌肉收缩向肌球蛋白ATP酶供应ATP的机制需要一个高度组织化的细胞系统。