Characterization of photolyase/blue-light receptor homologs in mouse and human cells
| Autor: | Shin Ichiro Kanno, Gijsbertus T. J. van der Horst, Kumiko Kobayashi, Masashi Takao, Bep Smit, Akira Yasui |
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| Přispěvatelé: | Molecular Genetics |
| Rok vydání: | 1998 |
| Předmět: |
animal structures
Molecular Sequence Data Nuclear Localization Signals Biology Antibodies law.invention Receptors G-Protein-Coupled Gene product Sepharose chemistry.chemical_compound Mice Species Specificity law Genetics Animals Drosophila Proteins Humans Amino Acid Sequence Photolyase Eye Proteins Gene Cellular localization In Situ Hybridization Fluorescence DNA Primers Base Sequence Flavoproteins Sequence Homology Amino Acid Chromosome Mapping DNA Molecular biology Immunohistochemistry Recombinant Proteins Cryptochromes Biochemistry chemistry Recombinant DNA Photoreceptor Cells Invertebrate Rabbits Deoxyribodipyrimidine Photo-Lyase Nuclear localization sequence Protein Binding Research Article |
| Zdroj: | Nucleic Acids Research, 26(22), 5086-5092. Oxford University Press |
| ISSN: | 0305-1048 |
| Popis: | We isolated and characterized mouse photolyase-like genes, mCRY1 (mPHLL1) and mCRY2 (mPHLL2), which belong to the photolyase family including plant blue-light receptors. The mCRY1 and mCRY2 genes are located on chromosome 10C and 2E, respectively, and are expressed in all mouse organs examined. We raised antibodies specific against each gene product using its C-terminal sequence, which differs completely between the genes. Immunofluorescent staining of cultured mouse cells revealed that mCRY1 is localized in mitochondria whereas mCRY2 was found mainly in the nucleus. The subcellular distribution of CRY proteins was confirmed by immunoblot analysis of fractionated mouse liver cell extracts. Using green fluorescent protein fused peptides we showed that the C-terminal region of the mouse CRY2 protein contains a unique nuclear localization signal, which is absent in the CRY1 protein. The N-terminal region of CRY1 was shown to contain the mitochondrial transport signal. Recombinant as well as native CRY1 proteins from mouse and human cells showed a tight binding activity to DNA Sepharose, while CRY2 protein did not bind to DNA Sepharose at all under the same condition as CRY1. The different cellular localization and DNA binding properties of the mammalian photolyase homologs suggest that despite the similarity in the sequence the two proteins have distinct function(s). |
| Databáze: | OpenAIRE |
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