Scallop lens Omega-crystallin (ALDH1A9): a novel tetrameric aldehyde dehydrogenase |
| |
Authors: | Horwitz Joseph Ding Linlin Vasiliou Vasilis Cantore Miriam Piatigorsky Joram |
| |
Institution: | Jules Stein Eye Institute, UCLA School of Medicine, Los Angeles, CA 90095-7008, USA. |
| |
Abstract: | Scallop eye lens Omega-crystallin is an inactive aldehyde dehydrogenase (ALDH1A9) related to cytoplasmic ALDH1A1 and mitochondrial ALDH2 that migrates by gel filtration chromatography as a homodimer. Because mammalian ALDH1A1 and ALDH2 are homotetramers, we investigated the native molecular mass of scallop Omega-crystallin by multi-angle laser light scattering. The results indicate that the scallop Omega-crystallin is a tetrameric, not a dimeric protein. Moreover, phylogenetic tree analysis shows that scallop Omega-crystallin clusters with the mitochondrial ALDH2 and ALDH1B1 rather than the cytoplasmic ALDH1A, yet it lacks the mitochondrial N-terminal leader sequence characteristic of the mitochondrial ALDHs. The mitochondrial grouping, enzymatic inactivity, and anomalous gel filtration behavior make scallop cytoplasmic Omega-crystallin an interesting protein for structural studies of evolutionary adaptations to become an enzyme-crystallin. |
| |
Keywords: | Lens crystallin Scallop Ω-crystallin Aldehyde dehydrogenase Molecular mass Multi-angle laser light scattering Mitochondria |
本文献已被 ScienceDirect PubMed 等数据库收录! |
|