Genomic organization and chromosomal localization of a new member of the murine interferon-induced guanylate-binding protein family.

An RNA species has been identified whose nucleotide sequence is closely related to the mRNA encoding the murine interferon (IFN)-induced guanylate-binding protein-1 (mGBP1) and an mRNA encoding an isoprenylated protein that is constitutively expressed in various organs in the rat. Sequence analysis of the gene encoding this newly identified RNA reveals that in its 5'-region it is identical to a DNA fragment reported to represent the 5'-region of a gene termed mGBP2. In light of this homology, we term this newly identified gene product mGBP2. mGBP2 is inducible following IFN treatment in animals bearing Gbp1a alleles, in which mGBP1 is transcriptionally upregulated by IFN treatment, as well as in animals bearing Gbp1b alleles, in which mGBP1 is not induced in response to IFN treatment. The genomic organizations of the genes encoding mGBP1 and mGBP2 are similar, and the nucleotide sequences of their IFN-responsive-like elements and their relative locations are conserved. Gbp1 and Gbp2 map to a genetically indistinguishable site on the distal arm of chromosome 3.

[1]  J. Sambrook,et al.  Molecular Cloning: A Laboratory Manual , 2001 .

[2]  G. Sen,et al.  Different subcellular localizations for the related interferon-induced GTPases, MuGBP-1 and MuGBP-2: implications for different functions? , 2000, Journal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research.

[3]  R. Maki,et al.  Induction of a prenylated 65‐kd protein in macrophages by interferon or lipopolysaccharide , 1995, Journal of leukocyte biology.

[4]  H. Ruffner,et al.  Interferon regulatory factor 1 is required for mouse Gbp gene activation by gamma interferon , 1995, Molecular and cellular biology.

[5]  D. Carey,et al.  Molecular cloning and characterization of an isoprenylated 67 kDa protein. , 1994, Biochimica et biophysica acta.

[6]  C. Nicolet,et al.  Promoter analysis of an interferon-inducible gene associated with macrophage activation. , 1994, Journal of immunology.

[7]  P. Lengyel,et al.  The interferon system. A bird's eye view of its biochemistry. , 1992, The Journal of biological chemistry.

[8]  W. Tate,et al.  Interferon induces tryptophanyl-tRNA synthetase expression in human fibroblasts. , 1991, The Journal of biological chemistry.

[9]  T. Wynn,et al.  Identification and characterization of a new gene family induced during macrophage activation. , 1991, Journal of immunology.

[10]  Yih-Shyun E. Cheng,et al.  Interferon-induced guanylate-binding proteins lack an N(T)KXD consensus motif and bind GMP in addition to GDP and GTP , 1991, Molecular and cellular biology.

[11]  A. Pingoud,et al.  The guanine‐nucleotide binding proteins EMBO‐NATO‐CEC advanced research workshop organized by L. Bosch, B. Kraal and A. Parmeggiani in Renesse, The Netherlands, August 6–11, 1988 , 1988, FEBS letters.

[12]  W. Merrick,et al.  GTP-binding domain: three consensus sequence elements with distinct spacing. , 1987, Proceedings of the National Academy of Sciences of the United States of America.

[13]  O. Haller,et al.  Interferon-induced guanylate-binding proteins: Mapping murine Gbp-1 locus to chromosome 3 , 1985 .

[14]  O. Haller,et al.  Genetic control of interferon action: mouse strain distribution and inheritance of an induced protein with guanylate-binding property. , 1984, Virology.

[15]  P. Staeheli,et al.  Different mRNAs induced by interferon in cells from inbred mouse strains A/J and A2G , 1983, Journal of virology.

[16]  P. Lengyel Biochemistry of interferons and their actions. , 1982, Annual review of biochemistry.