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N Adachi, DP Singh, T Shinohara, LT Chylack; Sequence Conservation of Lens Epithelium-Derived Growth Factor (LEDGF) . Invest. Ophthalmol. Vis. Sci. 2002;43(13):2341.
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Purpose: LEDGF enhances survival of many cells by binding to heat shock (HSE) and stress-related (STRE) elements to activate stress-related genes. To gain insight into LEDGF’s structure, evolutionary conservation, and ecliptic functional role, we determined a bovine LEDGF cDNA sequence. We also obtained LEDGF sequences of mouse, rat, chicken, pig, and fruit fly from Database and assessed their sequence homologies. Methods: A bovine brain cDNA library was screened with a [32P]-labeled human LEDGF cDNA probe. The cDNA clone was isolated, its DNA sequence was determined, and the polypeptide sequence was deduced. The LEDGF homologues of other species were obtained from the GenBank database using the BLAST program. For domain/motif structure analysis of the protein, the InterProScan and PSORT II analysis were used. Size of LEDGF mRNAs was determined by Northern blot analyses. Results: The entire bovine LEDGF polypeptide sequence was determined. The whole LEDGF sequences of human, bovine, and mouse were compared; ≷95% of the polypeptide sequence was conserved among them. LEDGF sequences contained several functional domains (e.g. seven nuclear localization signals (NLS), six DNA binding domains (three helix-turn-helixes, a coiled-coil, a basic leucine zipper, and an A-T hook), Tat-, PWWP-, and a TFS2N-domains). Among vertebrates we have studied, sequence conservation in each domain was extremely high. Size of mRNAs of LEDGF was found to be 3.4 kb. Conclusion: The high sequence conservations of these domains (NLS, Tat, a basic leucine zipper, and a helix-turn-helixes) are likely important for cell survival. .
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