Chromosomal Proteins HMGN3a and HMGN3b Regulate the Expression of Glycine Transporter 1

REFERENCES

• Adams, R. H., Sato K., Shimada S., Tohyama M., Puschel A. W., and Betz H.. 1995. Gene structure and glial expression of the glycine transporter GlyT1 in embryonic and adult rodents. J. Neurosci. 15:2524–2532.
   PubMed Web of Science ®Google Scholar
• Amano, T., Leu K., Yoshizato K., and Shi Y. B.. 2002. Thyroid hormone regulation of a transcriptional coactivator in Xenopus laevis: implication for a role in postembryonic tissue remodeling. Dev. Dyn. 223:526–535.
   PubMedGoogle Scholar
• Angus-Hill, M. L., A. Schlichter, D. Roberts, H. Erdjument-Bromage, P. Tempst, and B. R. Cairns. 2001. A Rsc3/Rsc30 zinc cluster dimer reveals novel roles for the chromatin remodeler RSC in gene expression and cell cycle control. Mol. Cell 7:741–751.
   PubMed Web of Science ®Google Scholar
• Birger, Y., Ito Y., West K. L., Landsman D., and Bustin M.. 2001. HMGN4, a new nucleosomal binding protein encoded by an intronless gene. DNA Cell Biol. 20:257–264.
   PubMedGoogle Scholar
• Birger, Y., West K. L., Postnikov Y. V., Lim J. H., Furusawa T., Wagner J. P., Laufer C. S., Kraemer K. H., and Bustin M.. 2003. Chromosomal protein HMGN1 enhances the rate of DNA repair in chromatin. EMBO J. 22:1665–1675.
   PubMed Web of Science ®Google Scholar
• Borowsky, B., and Hoffman B. J.. 1998. Analysis of a gene encoding two glycine transporter variants reveals alternative promoter usage and a novel gene structure. J. Biol. Chem. 273:29077–29085.
   PubMed Web of Science ®Google Scholar
• Borowsky, B., Mezey E., and Hoffman B. J.. 1993. Two glycine transporter variants with distinct localization in the CNS and peripheral tissues are encoded by a common gene. Neuron 10:851–863.
   PubMed Web of Science ®Google Scholar
• Bustin, M. 2001. Chromatin unfolding and activation by HMGN(*) chromosomal proteins. Trends Biochem. Sci. 26:431–437.
   PubMed Web of Science ®Google Scholar
• Bustin, M. 1999. Regulation of DNA-dependent activities by the functional motifs of the high-mobility-group chromosomal proteins. Mol. Cell. Biol. 19:5237–5246.
   PubMed Web of Science ®Google Scholar
• Catez, F., Brown D. T., Misteli T., and Bustin M.. 2002. Competition between histone H1 and HMGN proteins for chromatin binding sites. EMBO Rep. 3:760–766.
   PubMedGoogle Scholar
• Chung, J. H., Bell A. C., and Felsenfeld G.. 1997. Characterization of the chicken beta-globin insulator. Proc. Natl. Acad. Sci. USA 94:575–580.
   PubMed Web of Science ®Google Scholar
• Crippa, M. P., Alfonso P. J., and Bustin M.. 1992. Nucleosome core binding region of chromosomal protein HMG-17 acts as an independent functional domain. J. Mol. Biol. 228:442–449.
   PubMedGoogle Scholar
• Crippa, M. P., Trieschmann L., Alfonso P. J., Wolffe A. P., and Bustin M.. 1993. Deposition of chromosomal protein HMG-17 during replication affects the nucleosomal ladder and transcriptional potential of nascent chromatin. EMBO J. 12:3855–3864.
   PubMedGoogle Scholar
• Ding, H. F., Bustin M., and Hansen U.. 1997. Alleviation of histone H1-mediated transcriptional repression and chromatin compaction by the acidic activation region in chromosomal protein HMG-14. Mol. Cell. Biol. 17:5843–5855.
   PubMedGoogle Scholar
• Ding, H. F., Rimsky S., Batson S. C., Bustin M., and Hansen U.. 1994. Stimulation of RNA polymerase II elongation by chromosomal protein HMG-14. Science 265:796–799.
   PubMedGoogle Scholar
• Dorbic, T., and Wittig B.. 1987. Chromatin from transcribed genes contains HMG17 only downstream from the starting point of transcription. EMBO J. 6:2393–2399.
   PubMedGoogle Scholar
• Dorbic, T., and Wittig B.. 1986. Isolation of oligonucleosomes from active chromatin using HMG17-specific monoclonal antibodies. Nucleic Acids Res. 14:3363–3376.
   PubMedGoogle Scholar
• Fischle, W., Wang Y., and Allis C. D.. 2003. Histone and chromatin cross-talk. Curr. Opin. Cell Biol. 15:172–183.
   PubMed Web of Science ®Google Scholar
• Goebel, D. J. 1996. Quantitative gene expression of two types of glycine transporter in the rat central nervous system. Brain Res. Mol. Brain Res. 40:139–142.
   PubMedGoogle Scholar
• Goodwin, G. H., Mathew C. G., Wright C. A., Venkov C. D., and Johns E. W.. 1979. Analysis of the high mobility group proteins associated with salt-soluble nucleosomes. Nucleic Acids Res. 7:1815–1835.
   PubMedGoogle Scholar
• Hegde, P., Qi R., Abernathy K., Gay C., Dharap S., Gaspard R., Hughes J. E., Snesrud E., Lee N., and Quackenbush J.. 2000. A concise guide to cDNA microarray analysis. BioTechniques 29:548–550, 552-554, 556.
   PubMed Web of Science ®Google Scholar
• Hock, R., Wilde F., Scheer U., and Bustin M.. 1998. Dynamic relocation of chromosomal protein HMG-17 in the nucleus is dependent on transcriptional activity. EMBO J. 17:6992–7001.
   PubMedGoogle Scholar
• Ito, Y., and Bustin M.. 2002. Immunohistochemical localization of the nucleosome-binding protein HMGN3 in mouse brain. J. Histochem. Cytochem. 50:1273–1275.
   PubMedGoogle Scholar
• Jenuwein, T., and Allis C. D.. 2001. Translating the histone code. Science 293:1074–1080.
   PubMed Web of Science ®Google Scholar
• Kim, K. M., Kingsmore S. F., Han H., Yang-Feng T. L., Godinot N., Seldin M. F., Caron M. G., and Giros B.. 1994. Cloning of the human glycine transporter type 1: molecular and pharmacological characterization of novel isoform variants and chromosomal localization of the gene in the human and mouse genomes. Mol. Pharmacol. 45:608–617.
   PubMed Web of Science ®Google Scholar
• Lee, J. W., Choi H. S., Gyuris J., Brent R., and Moore D. D.. 1995. Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with thyroid hormone receptor. Mol. Endocrinol. 9:243–254.
   PubMed Web of Science ®Google Scholar
• Lehtonen, S., and Lehtonen E.. 2001. HMG-17 is an early marker of inductive interactions in the developing mouse kidney. Differentiation 67:154–163.
   PubMedGoogle Scholar
• Lehtonen, S., Olkkonen V. M., Stapleton M., Zerial M., and Lehtonen E.. 1998. HMG-17, a chromosomal non-histone protein, shows developmental regulation during organogenesis. Int. J. Dev. Biol. 42:775–782.
   PubMedGoogle Scholar
• Lim, J. H., Bustin M., Ogryzko V. V., and Postnikov Y. V.. 2002. Metastable macromolecular complexes containing high mobility group nucleosome-binding chromosomal proteins in HeLa nuclei. J. Biol. Chem. 277:20774–20782.
   PubMedGoogle Scholar
• Litt, M. D., Simpson M., Recillas-Targa F., Prioleau M. N., and Felsenfeld G.. 2001. Transitions in histone acetylation reveal boundaries of three separately regulated neighboring loci. EMBO J. 20:2224–2235.
   PubMedGoogle Scholar
• Lopez-Corcuera, B., A. Geerlings, and C. Aragon. 2001. Glycine neurotransmitter transporters: an update. Mol. Membr. Biol. 18:13–20.
   PubMed Web of Science ®Google Scholar
• Martens, J. A., and Winston F.. 2003. Recent advances in understanding chromatin remodeling by Swi/Snf complexes. Curr. Opin. Genet. Dev. 13:136–142.
   PubMed Web of Science ®Google Scholar
• Menger, N., Pow D. V., and Wassle H.. 1998. Glycinergic amacrine cells of the rat retina. J. Comp. Neurol. 401:34–46.
   PubMed Web of Science ®Google Scholar
• Orlando, V., Strutt H., and Paro R.. 1997. Analysis of chromatin structure by in vivo formaldehyde cross-linking. Methods 11:205–214.
   PubMed Web of Science ®Google Scholar
• Paranjape, S. M., Krumm A., and Kadonaga J. T.. 1995. HMG17 is a chromatin-specific transcriptional coactivator that increases the efficiency of transcription initiation. Genes Dev. 9:1978–1991.
   PubMedGoogle Scholar
• Pash, J., Popescu N., Matocha M., Rapoport S., and Bustin M.. 1990. Chromosomal protein HMG-14 gene maps to the Down syndrome region of human chromosome 21 and is overexpressed in mouse trisomy 16. Proc. Natl. Acad. Sci. USA 87:3836–3840.
   PubMedGoogle Scholar
• Phair, R. D., and Misteli T.. 2000. High mobility of proteins in the mammalian cell nucleus. Nature 404:604–609.
   PubMed Web of Science ®Google Scholar
• Postnikov, Y. V., Herrera J. E., Hock R., Scheer U., and Bustin M.. 1997. Clusters of nucleosomes containing chromosomal protein HMG-17 in chromatin. J. Mol. Biol. 274:454–465.
   PubMedGoogle Scholar
• Postnikov, Y. V., Shick V. V., Belyavsky A. V., Khrapko K. R., Brodolin K. L., Nikolskaya T. A., and Mirzabekov A. D.. 1991. Distribution of high mobility group proteins 1/2, E and 14/17 and linker histones H1 and H5 on transcribed and non-transcribed regions of chicken erythrocyte chromatin. Nucleic Acids Res. 19:717–725.
   PubMedGoogle Scholar
• Postnikov, Y. V., Trieschmann L., Rickers A., and Bustin M.. 1995. Homodimers of chromosomal proteins HMG-14 and HMG-17 in nucleosome cores. J. Mol. Biol. 252:423–432.
   PubMedGoogle Scholar
• Pow, D. V., and Hendrickson A. E.. 1999. Distribution of the glycine transporter glyt-1 in mammalian and nonmammalian retinae. Vis. Neurosci. 16:231–239.
   PubMed Web of Science ®Google Scholar
• Pow, D. V., and Hendrickson A. E.. 2000. Expression of glycine and the glycine transporter glyt-1 in the developing rat retina. Vis. Neurosci. 17:1–9.
   PubMedGoogle Scholar
• Reed, N. A., Oh D. J., Czymmek K. J., and Duncan M. K.. 2001. An immunohistochemical method for the detection of proteins in the vertebrate lens. J. Immunol. Methods 253:243–252.
   PubMedGoogle Scholar
• Shen, X., and Gorovsky M. A.. 1996. Linker histone H1 regulates specific gene expression but not global transcription in vivo. Cell 86:475–483.
   PubMedGoogle Scholar
• Shirakawa, H., Herrera J. E., Bustin M., and Postnikov Y.. 2000. Targeting of high mobility group-14/-17 proteins in chromatin is independent of DNA sequence. J. Biol. Chem. 275:37937–37944.
   PubMedGoogle Scholar
• Trieschmann, L., Alfonso P. J., Crippa M. P., Wolffe A. P., and Bustin M.. 1995. Incorporation of chromosomal proteins HMG-14/HMG-17 into nascent nucleosomes induces an extended chromatin conformation and enhances the utilization of active transcription complexes. EMBO J. 14:1478–1489.
   PubMedGoogle Scholar
• Trieschmann, L., Postnikov Y. V., Rickers A., and Bustin M.. 1995. Modular structure of chromosomal proteins HMG-14 and HMG-17: definition of a transcriptional enhancement domain distinct from the nucleosomal binding domain. Mol. Cell. Biol. 15:6663–6669.
   PubMedGoogle Scholar
• Turner, B. M. 2002. Cellular memory and the histone code. Cell 111:285–291.
   PubMed Web of Science ®Google Scholar
• Vestner, B., Bustin M., and Gruss C.. 1998. Stimulation of replication efficiency of a chromatin template by chromosomal protein HMG-17. J. Biol. Chem. 273:9409–9414.
   PubMedGoogle Scholar
• Weigmann, N., Trieschmann L., and Bustin M.. 1997. Enhancement of the transcription potential of nascent chromatin by chromosomal proteins HMG-14/-17 is coupled to nucleosome assembly and not DNA synthesis. DNA Cell Biol. 16:1207–1216.
   PubMedGoogle Scholar
• Weisbrod, S., Groudine M., and Weintraub H.. 1980. Interaction of HMG 14 and 17 with actively transcribed genes. Cell 19:289–301.
   PubMed Web of Science ®Google Scholar
• Weisbrod, S., and Weintraub H.. 1981. Isolation of actively transcribed nucleosomes using immobilized HMG 14 and 17 and an analysis of alpha-globin chromatin. Cell 23:391–400.
   PubMed Web of Science ®Google Scholar
• West, K. L., Ito Y., Birger Y., Postnikov Y., Shirakawa H., and Bustin M.. 2001. HMGN3a and HMGN3b, two protein isoforms with a tissue-specific expression pattern, expand the cellular repertoire of nucleosome-binding proteins. J. Biol. Chem. 276:25959–25969.
   PubMedGoogle Scholar
• Zafra, F., Aragon C., Olivares L., Danbolt N. C., Gimenez C., and Storm-Mathisen J.. 1995. Glycine transporters are differentially expressed among CNS cells. J. Neurosci. 15:3952–3969.
   PubMed Web of Science ®Google Scholar