Nucleic Acids Research, 1991, Vol. 19, No. 5 1035-1040
© 1991
MOLECULAR BIOLOGY |
The human ubiquitin-52 amino acid fusion protein gene shares several structural features with mammalian ribosomal protein genes
Human Genetics Group, Division of Clinical Sciences, John Curtin School of Medical Research, Australian National University P0 Box 334, Canberra, ACT 2601, Australia
* To whom correspondence should be addressed
Received December 13, 1990. Accepted January 28, 1991.
Complementary DNA clones encoding ubiqultin fused to a 52 amino acid tall protein were Isolated from human placental and adrenal gland cDNA libraries. The deduced human 52 amino acid tail protein is very similar to the homologous protein from other species, including the conservation of the putative metal-binding, nucleic acid-binding domain observed in these proteins. Northern blot analysis with a tail-specific probe indicated that the previously identified UbA mRNA species most likely represents comigrating transcripts of the 52 amino acid tall (UbA and 80 amino acid tall (UbA80) ubiqultin fusion genes. The UbA52 gene was isolated from a human genomic library and consists of five exons distributed over 3400 base pairs. One intron is in the 5' non-coding region, two interrupt the single ubiquitin coding unit, and the fourth Intron is within the tail coding region. Several members of the Alu family of repetitive DNA are associated with the gene. The UbA52 promoter has several features in common with mammalian ribosomal protein genes, including its location in a CpG-rlch island, Initiation of transcription within a polypyilmidine tract, the lack of a consensus TATA motif, and the presence of Spi binding sites, observations that are consistent with the recent Identification of the ubiqultin free tail proteins as ribosomal proteins. Thus, in spite of Its unusual feature of being translationally fused to ubiquitin, the 52 amino acid tail ribosomai protein is expressed from a structurally typical ribosomal protein gene.
+Present address: Department of Biology, Room 16-520, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
![]()
CiteULike
Connotea
Del.icio.us What's this?
This article has been cited by other articles:
![]() |
K.-Y. Ryu, J. C. Garza, X.-Y. Lu, G. S. Barsh, and R. R. Kopito Hypothalamic neurodegeneration and adult-onset obesity in mice lacking the Ubb polyubiquitin gene PNAS, March 11, 2008; 105(10): 4016 - 4021. [Abstract] [Full Text] [PDF] |
||||
![]() |
K.-Y. Ryu, S. A. Sinnar, L. G. Reinholdt, S. Vaccari, S. Hall, M. A. Garcia, T. S. Zaitseva, D. M. Bouley, K. Boekelheide, M. A. Handel, et al. The Mouse Polyubiquitin Gene Ubb Is Essential for Meiotic Progression Mol. Cell. Biol., February 1, 2008; 28(3): 1136 - 1146. [Abstract] [Full Text] [PDF] |
||||
![]() |
X.-L. Liu, J.-Y. Yuan, J.-W. Zhang, X.-H. Zhang, and R.-X. Wang Differential gene expression in human hematopoietic stem cells specified toward erythroid, megakaryocytic, and granulocytic lineage J. Leukoc. Biol., October 1, 2007; 82(4): 986 - 1002. [Abstract] [Full Text] [PDF] |
||||
![]() |
R. Scherz-Shouval, Y. Sagiv, H. Shorer, and Z. Elazar The COOH Terminus of GATE-16, an Intra-Golgi Transport Modulator, Is Cleaved by the Human Cysteine Protease HsApg4A J. Biol. Chem., April 11, 2003; 278(16): 14053 - 14058. [Abstract] [Full Text] [PDF] |
||||
![]() |
L. Sun, X. Pan, J. Wada, C. S. Haas, R. P. Wuthrich, F. R. Danesh, S. S. Chugh, and Y. S. Kanwar Isolation and Functional Analysis of Mouse UbA52 Gene and Its Relevance to Diabetic Nephropathy J. Biol. Chem., August 9, 2002; 277(33): 29953 - 29962. [Abstract] [Full Text] [PDF] |
||||
![]() |
D. D. Desai and T. N. Marion Induction of anti-DNA antibody with DNA-peptide complexes Int. Immunol., November 1, 2000; 12(11): 1569 - 1578. [Abstract] [Full Text] [PDF] |
||||
![]() |
M. Nenoi, K. Mita, S. Ichimura, and A. Kawano Higher Frequency of Concerted Evolutionary Events in Rodents Than in Man at the Polyubiquitin Gene VNTR Locus Genetics, February 1, 1998; 148(2): 867 - 876. [Abstract] [Full Text] [PDF] |
||||
![]() |
R. K. Vadlamudi, I. Joung, J. L. Strominger, and J. Shin p62, a Phosphotyrosine-independent Ligand of the SH2 Domain of p56lck, Belongs to a New Class of Ubiquitin-binding Proteins J. Biol. Chem., August 23, 1996; 271(34): 20235 - 20237. [Abstract] [Full Text] [PDF] |
||||
![]() |
R. T. Baker, N. A. Williamson, and R. E.H. Wettenhall The Yeast Homolog of Mammalian Ribosomal Protein S30 Is Expressed from a Duplicated Gene without a Ubiquitin-like Protein Fusion Sequence. EVOLUTIONARY IMPLICATIONS J. Biol. Chem., June 7, 1996; 271(23): 13549 - 13555. [Abstract] [Full Text] [PDF] |
||||





