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• W2015757949 abstract "Transcription factors of the ONECUT class, whose prototype is hepatocyte nuclear factor (HNF)-6, are characterized by the presence of a single cut domain and by a peculiar homeodomain (Lannoy, V. J., Bürglin, T. R., Rousseau, G. G., and Lemaigre, F. P. (1998) J. Biol. Chem. 273, 13552–13562). We report here the identification and characterization of human OC-2, the second mammalian member of this class. TheOC-2 gene is located on human chromosome 18. The distribution of OC-2 mRNA in humans is tissue-restricted, the strongest expression being detected in the liver and skin. The amino acid sequence of OC-2 contains several regions of high similarity to HNF-6. The recognition properties of OC-2 for binding sites present in regulatory regions of liver-expressed genes differ from, but overlap with, those of HNF-6. Like HNF-6, OC-2 stimulates transcription of the hnf-3βgene in transient transfection experiments, suggesting that OC-2 participates in the network of transcription factors required for liver differentiation and metabolism. Transcription factors of the ONECUT class, whose prototype is hepatocyte nuclear factor (HNF)-6, are characterized by the presence of a single cut domain and by a peculiar homeodomain (Lannoy, V. J., Bürglin, T. R., Rousseau, G. G., and Lemaigre, F. P. (1998) J. Biol. Chem. 273, 13552–13562). We report here the identification and characterization of human OC-2, the second mammalian member of this class. TheOC-2 gene is located on human chromosome 18. The distribution of OC-2 mRNA in humans is tissue-restricted, the strongest expression being detected in the liver and skin. The amino acid sequence of OC-2 contains several regions of high similarity to HNF-6. The recognition properties of OC-2 for binding sites present in regulatory regions of liver-expressed genes differ from, but overlap with, those of HNF-6. Like HNF-6, OC-2 stimulates transcription of the hnf-3βgene in transient transfection experiments, suggesting that OC-2 participates in the network of transcription factors required for liver differentiation and metabolism. The identification of transcription factors has provided insight into the mechanisms of the control of gene expression. Some of these factors contain a DNA-binding region called the homeodomain. The homeodomain proteins are evolutionarily conserved and play an important role in cell differentiation and in morphogenesis (1Kenyon C. Cell. 1994; 78: 175-180Abstract Full Text PDF PubMed Scopus (100) Google Scholar, 2Lawrence P.A. Morata G. Cell. 1994; 78: 181-189Abstract Full Text PDF PubMed Scopus (244) Google Scholar, 3Krumlauf R. Cell. 1994; 78: 191-201Abstract Full Text PDF PubMed Scopus (1730) Google Scholar, 4$$Google Scholar). Several homeodomain proteins contain a second type of DNA-binding domain. This is the case for the proteins of the CUT superclass, in which the second DNA-binding domain is called cut because it was initially described in the Drosophila CUT protein (5Blochlinger K. Bodmer R. Jack J. Jan L.Y. Jan Y.N. Nature. 1988; 333: 629-634Crossref PubMed Scopus (222) Google Scholar, 6Harada R. Dufort D. Denis-Larose C. Nepveu A. J. Biol. Chem. 1994; 269: 2062-2067Abstract Full Text PDF PubMed Google Scholar, 7Andrés V. Chiara M.D. Mahdavi V. Genes Dev. 1994; 8: 245-257Crossref PubMed Scopus (96) Google Scholar). The CUT superclass comprises three classes (8Lannoy V.J. Bürglin T.R. Rousseau G.G. Lemaigre F.P. J. Biol. Chem. 1998; 273: 13552-13562Abstract Full Text Full Text PDF PubMed Scopus (92) Google Scholar). The CUX class, whose members have three cut domains, includes the Drosophila CUT protein and its mammalian homologs, namely human CDP, rat CDP-2, dog CLOX, and mouse CUX and CUX-2. The SATB class, whose members have two cut domains, includes the human homeodomain proteins called matrix attachment region-binding proteins or SATB (specialAT-rich binding) proteins. A third class, called ONECUT because its members have a single cut domain, was identified (8Lannoy V.J. Bürglin T.R. Rousseau G.G. Lemaigre F.P. J. Biol. Chem. 1998; 273: 13552-13562Abstract Full Text Full Text PDF PubMed Scopus (92) Google Scholar) thanks to the cloning of rat hepatocyte nuclear factor-6 (HNF-6) 1The abbreviations used are: HNF, hepatocyte nuclear factor; ORF, open reading frame; RT-PCR, reverse transcription-polymerase chain reaction; TTR, transthyretin; PEPCK, phosphoenolpyruvate carboxykinase; GRU, glucocorticoid-responsive unit; bp, base pair(s); CORD, cone-rod dystrophy. 1The abbreviations used are: HNF, hepatocyte nuclear factor; ORF, open reading frame; RT-PCR, reverse transcription-polymerase chain reaction; TTR, transthyretin; PEPCK, phosphoenolpyruvate carboxykinase; GRU, glucocorticoid-responsive unit; bp, base pair(s); CORD, cone-rod dystrophy.(9Lemaigre F.P. Durviaux S.M. Truong O. Lannoy V.J. Hsuan J.J. Rousseau G.G. Proc. Natl. Acad. Sci. U. S. A. 1996; 93: 9460-9464Crossref PubMed Scopus (128) Google Scholar). The ONECUT class includes mammalian HNF-6 and four Caenorhabditis elegans cDNAs or open reading frames (ORFs) (8Lannoy V.J. Bürglin T.R. Rousseau G.G. Lemaigre F.P. J. Biol. Chem. 1998; 273: 13552-13562Abstract Full Text Full Text PDF PubMed Scopus (92) Google Scholar).The proteins of the ONECUT class are characterized not only by their single cut domain, but also by a homeodomain with a peculiar amino acid composition. Homeodomains, which are 60 residues long, are organized in three α-helices (for a review on homeodomain-DNA interactions, see Refs. 10Kornberg T.B. J. Biol. Chem. 1993; 268: 26813-26816Abstract Full Text PDF PubMed Google Scholar, 11Gehring W.J. Qian Y.Q. Billeter M. Furukubo-Tokunaga K. Schier A.F. Resendez-Perez D. Affolter M. Otting G. Wüthrich K. Cell. 1994; 78: 211-223Abstract Full Text PDF PubMed Scopus (693) Google Scholar, 12Wolberger C. Cur. Opin. Struct. Biol. 1996; 6: 62-68Crossref PubMed Scopus (116) Google Scholar). The third helix, called the recognition helix, contacts the DNA and is crucial for sequence-specific binding. Within this helix, residue 48 is part of a hydrophobic core. Whereas residue 48 is a tryptophan in all known homeodomains, it is a phenylalanine in the ONECUT proteins. Residue 50 is also located in the recognition helix. Mutations at this position often lead to changes in the sequence specificity of DNA binding (13Hanes S.D. Brent R. Cell. 1989; 57: 1275-1283Abstract Full Text PDF PubMed Scopus (379) Google Scholar, 14Ades S.E. Sauer R.T. Biochemistry. 1994; 33: 9187-9194Crossref PubMed Scopus (111) Google Scholar, 15Stepchenko A.G. Luchina N.N. Pankratova E.V. Nucleic Acids Res. 1997; 25: 2847-2853Crossref PubMed Scopus (30) Google Scholar). This is consistent with the crystallization data that demonstrate that the amino acid at position 50 is in contact with bases (for a review, see Ref. 16Treisman J. Harris E. Wilson D. Desplan C. Bioessays. 1992; 14: 145-150Crossref PubMed Scopus (100) Google Scholar). In the ONECUT proteins, a methionine is found at position 50. This amino acid is never found at this position in other homeodomains.Our previous experiments showed that HNF-6 can bind to a number of DNA sites, which differ slightly in terms of sequence, and that the cut domain is required for binding of HNF-6 to all the sites tested (8Lannoy V.J. Bürglin T.R. Rousseau G.G. Lemaigre F.P. J. Biol. Chem. 1998; 273: 13552-13562Abstract Full Text Full Text PDF PubMed Scopus (92) Google Scholar). These experiments ascribed a dual role to the peculiar homeodomain of HNF-6. They showed that this domain is involved in DNA binding, but only for a subset of the sites recognized by HNF-6. They also showed that the homeodomain is involved in transcriptional activation, but only of those genes for which the binding of HNF-6 does not require its homeodomain. By mutational analysis, we demonstrated that phenylalanine 48 and methionine 50 play a role in this transcriptional activating function of the HNF-6 homeodomain (8Lannoy V.J. Bürglin T.R. Rousseau G.G. Lemaigre F.P. J. Biol. Chem. 1998; 273: 13552-13562Abstract Full Text Full Text PDF PubMed Scopus (92) Google Scholar). This work indicated that the linker region between the cut domain and homeodomain of HNF-6 is important for DNA binding (8Lannoy V.J. Bürglin T.R. Rousseau G.G. Lemaigre F.P. J. Biol. Chem. 1998; 273: 13552-13562Abstract Full Text Full Text PDF PubMed Scopus (92) Google Scholar). We identified two rat isoforms (HNF-6α and HNF-6β) that originate from the same gene by alternative splicing (17Rastegar M. Szpirer C. Rousseau G.G. Lemaigre F.P. Biochem. J. 1998; 334: 565-569Crossref PubMed Scopus (23) Google Scholar). HNF-6β (491 residues) is identical to HNF-6α (465 residues), except that it contains an insert of 26 amino acids in the linker region. These two isoforms differ in DNA binding specificity and kinetics (8Lannoy V.J. Bürglin T.R. Rousseau G.G. Lemaigre F.P. J. Biol. Chem. 1998; 273: 13552-13562Abstract Full Text Full Text PDF PubMed Scopus (92) Google Scholar).As mentioned above, the ONECUT class contains several C. elegans members, but only one mammalian member, namely HNF-6. The DNA-binding domains of these C. elegans proteins display DNA binding properties similar to those of HNF-6 (8Lannoy V.J. Bürglin T.R. Rousseau G.G. Lemaigre F.P. J. Biol. Chem. 1998; 273: 13552-13562Abstract Full Text Full Text PDF PubMed Scopus (92) Google Scholar). This indicates that these properties have been evolutionarily conserved and are therefore important for basic regulatory processes that are common to nematodes and mammals. The existence of several members of the ONECUT class inC. elegans prompted us to search for mammalian members of this class that are distinct from HNF-6. We describe here a new member, which we call OC-2, of the ONECUT class. The identification of transcription factors has provided insight into the mechanisms of the control of gene expression. Some of these factors contain a DNA-binding region called the homeodomain. The homeodomain proteins are evolutionarily conserved and play an important role in cell differentiation and in morphogenesis (1Kenyon C. Cell. 1994; 78: 175-180Abstract Full Text PDF PubMed Scopus (100) Google Scholar, 2Lawrence P.A. Morata G. Cell. 1994; 78: 181-189Abstract Full Text PDF PubMed Scopus (244) Google Scholar, 3Krumlauf R. Cell. 1994; 78: 191-201Abstract Full Text PDF PubMed Scopus (1730) Google Scholar, 4$$Google Scholar). Several homeodomain proteins contain a second type of DNA-binding domain. This is the case for the proteins of the CUT superclass, in which the second DNA-binding domain is called cut because it was initially described in the Drosophila CUT protein (5Blochlinger K. Bodmer R. Jack J. Jan L.Y. Jan Y.N. Nature. 1988; 333: 629-634Crossref PubMed Scopus (222) Google Scholar, 6Harada R. Dufort D. Denis-Larose C. Nepveu A. J. Biol. Chem. 1994; 269: 2062-2067Abstract Full Text PDF PubMed Google Scholar, 7Andrés V. Chiara M.D. Mahdavi V. Genes Dev. 1994; 8: 245-257Crossref PubMed Scopus (96) Google Scholar). The CUT superclass comprises three classes (8Lannoy V.J. Bürglin T.R. Rousseau G.G. Lemaigre F.P. J. Biol. Chem. 1998; 273: 13552-13562Abstract Full Text Full Text PDF PubMed Scopus (92) Google Scholar). The CUX class, whose members have three cut domains, includes the Drosophila CUT protein and its mammalian homologs, namely human CDP, rat CDP-2, dog CLOX, and mouse CUX and CUX-2. The SATB class, whose members have two cut domains, includes the human homeodomain proteins called matrix attachment region-binding proteins or SATB (specialAT-rich binding) proteins. A third class, called ONECUT because its members have a single cut domain, was identified (8Lannoy V.J. Bürglin T.R. Rousseau G.G. Lemaigre F.P. J. Biol. Chem. 1998; 273: 13552-13562Abstract Full Text Full Text PDF PubMed Scopus (92) Google Scholar) thanks to the cloning of rat hepatocyte nuclear factor-6 (HNF-6) 1The abbreviations used are: HNF, hepatocyte nuclear factor; ORF, open reading frame; RT-PCR, reverse transcription-polymerase chain reaction; TTR, transthyretin; PEPCK, phosphoenolpyruvate carboxykinase; GRU, glucocorticoid-responsive unit; bp, base pair(s); CORD, cone-rod dystrophy. 1The abbreviations used are: HNF, hepatocyte nuclear factor; ORF, open reading frame; RT-PCR, reverse transcription-polymerase chain reaction; TTR, transthyretin; PEPCK, phosphoenolpyruvate carboxykinase; GRU, glucocorticoid-responsive unit; bp, base pair(s); CORD, cone-rod dystrophy.(9Lemaigre F.P. Durviaux S.M. Truong O. Lannoy V.J. Hsuan J.J. Rousseau G.G. Proc. Natl. Acad. Sci. U. S. A. 1996; 93: 9460-9464Crossref PubMed Scopus (128) Google Scholar). The ONECUT class includes mammalian HNF-6 and four Caenorhabditis elegans cDNAs or open reading frames (ORFs) (8Lannoy V.J. Bürglin T.R. Rousseau G.G. Lemaigre F.P. J. Biol. Chem. 1998; 273: 13552-13562Abstract Full Text Full Text PDF PubMed Scopus (92) Google Scholar). The proteins of the ONECUT class are characterized not only by their single cut domain, but also by a homeodomain with a peculiar amino acid composition. Homeodomains, which are 60 residues long, are organized in three α-helices (for a review on homeodomain-DNA interactions, see Refs. 10Kornberg T.B. J. Biol. Chem. 1993; 268: 26813-26816Abstract Full Text PDF PubMed Google Scholar, 11Gehring W.J. Qian Y.Q. Billeter M. Furukubo-Tokunaga K. Schier A.F. Resendez-Perez D. Affolter M. Otting G. Wüthrich K. Cell. 1994; 78: 211-223Abstract Full Text PDF PubMed Scopus (693) Google Scholar, 12Wolberger C. Cur. Opin. Struct. Biol. 1996; 6: 62-68Crossref PubMed Scopus (116) Google Scholar). The third helix, called the recognition helix, contacts the DNA and is crucial for sequence-specific binding. Within this helix, residue 48 is part of a hydrophobic core. Whereas residue 48 is a tryptophan in all known homeodomains, it is a phenylalanine in the ONECUT proteins. Residue 50 is also located in the recognition helix. Mutations at this position often lead to changes in the sequence specificity of DNA binding (13Hanes S.D. Brent R. Cell. 1989; 57: 1275-1283Abstract Full Text PDF PubMed Scopus (379) Google Scholar, 14Ades S.E. Sauer R.T. Biochemistry. 1994; 33: 9187-9194Crossref PubMed Scopus (111) Google Scholar, 15Stepchenko A.G. Luchina N.N. Pankratova E.V. Nucleic Acids Res. 1997; 25: 2847-2853Crossref PubMed Scopus (30) Google Scholar). This is consistent with the crystallization data that demonstrate that the amino acid at position 50 is in contact with bases (for a review, see Ref. 16Treisman J. Harris E. Wilson D. Desplan C. Bioessays. 1992; 14: 145-150Crossref PubMed Scopus (100) Google Scholar). In the ONECUT proteins, a methionine is found at position 50. This amino acid is never found at this position in other homeodomains. Our previous experiments showed that HNF-6 can bind to a number of DNA sites, which differ slightly in terms of sequence, and that the cut domain is required for binding of HNF-6 to all the sites tested (8Lannoy V.J. Bürglin T.R. Rousseau G.G. Lemaigre F.P. J. Biol. Chem. 1998; 273: 13552-13562Abstract Full Text Full Text PDF PubMed Scopus (92) Google Scholar). These experiments ascribed a dual role to the peculiar homeodomain of HNF-6. They showed that this domain is involved in DNA binding, but only for a subset of the sites recognized by HNF-6. They also showed that the homeodomain is involved in transcriptional activation, but only of those genes for which the binding of HNF-6 does not require its homeodomain. By mutational analysis, we demonstrated that phenylalanine 48 and methionine 50 play a role in this transcriptional activating function of the HNF-6 homeodomain (8Lannoy V.J. Bürglin T.R. Rousseau G.G. Lemaigre F.P. J. Biol. Chem. 1998; 273: 13552-13562Abstract Full Text Full Text PDF PubMed Scopus (92) Google Scholar). This work indicated that the linker region between the cut domain and homeodomain of HNF-6 is important for DNA binding (8Lannoy V.J. Bürglin T.R. Rousseau G.G. Lemaigre F.P. J. Biol. Chem. 1998; 273: 13552-13562Abstract Full Text Full Text PDF PubMed Scopus (92) Google Scholar). We identified two rat isoforms (HNF-6α and HNF-6β) that originate from the same gene by alternative splicing (17Rastegar M. Szpirer C. Rousseau G.G. Lemaigre F.P. Biochem. J. 1998; 334: 565-569Crossref PubMed Scopus (23) Google Scholar). HNF-6β (491 residues) is identical to HNF-6α (465 residues), except that it contains an insert of 26 amino acids in the linker region. These two isoforms differ in DNA binding specificity and kinetics (8Lannoy V.J. Bürglin T.R. Rousseau G.G. Lemaigre F.P. J. Biol. Chem. 1998; 273: 13552-13562Abstract Full Text Full Text PDF PubMed Scopus (92) Google Scholar). As mentioned above, the ONECUT class contains several C. elegans members, but only one mammalian member, namely HNF-6. The DNA-binding domains of these C. elegans proteins display DNA binding properties similar to those of HNF-6 (8Lannoy V.J. Bürglin T.R. Rousseau G.G. Lemaigre F.P. J. Biol. Chem. 1998; 273: 13552-13562Abstract Full Text Full Text PDF PubMed Scopus (92) Google Scholar). This indicates that these properties have been evolutionarily conserved and are therefore important for basic regulatory processes that are common to nematodes and mammals. The existence of several members of the ONECUT class inC. elegans prompted us to search for mammalian members of this class that are distinct from HNF-6. We describe here a new member, which we call OC-2, of the ONECUT class. We thank J.-M. Garnier for the HeLa cell cDNA library, J. Nathans for the retina cDNA library, I. Davidson for pXJ42, R. Costa for pHNF6/HNF3β(6×)-TATA-luc, F. Brasseur for human RNA samples, the United Kingdom Human Genome Mapping Project Resource Center for the IMAGE clone 566080, and S. Durviaux and S. Neou for expert technical assistance." @default.
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• W2015757949 title "OC-2, a Novel Mammalian Member of the ONECUT Class of Homeodomain Transcription Factors Whose Function in Liver Partially Overlaps with That of Hepatocyte Nuclear Factor-6" @default.
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