Skip Navigation

This Article
Right arrow Print PDF (1427K)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (9)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by King, D.
Right arrow Articles by Lingrel, J. B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by King, D.
Right arrow Articles by Lingrel, J. B.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1986, Vol. 14, No. 13 5159-5170
© 1986


Articles

Amino acid sequence of the testosterone-regulated mouse kidney RP2 protein deduced from its complementary DNA sequence

Donna King1,, Y.Henry Sun2,3 and Jerry B. Lingrel*,

Department of Microbiology and Molecular Genetics, and Program in Developmental Biology, University of Cincinnati College of Medicine Cincinnati, OH 45267 3Division of Biology, California Institute of Technology Pasadena, CA 91125, USA

*To whom reprint requests should be addressed

Received May 5, 1986. Accepted June 11, 1986.

The major forms of testosterone-regulated RP2 messenger RNA (also known as MAK mRNA and pMK908) in the mouse kidney were characterized by examining cDNA and genomic clones. Three sizes of RP2 mRNA are detected by Northern blot analysis and these were shown to result from polyadenylation at three distinct sites within the primary transcript of this single-copy gene. The complete RP2 mRNA sequence was obtained from overlapping cDNA clones, revealing an open reading frame of 357 amino acids that corresponds to a protein of 40,385 daltons. The detection of RP2 mRNA in all tissues examined to date suggests that the RP2 protein may function in a housekeeping role In all cells. This is supported by the finding of a high percentage of G+C residues at the 5' end of the gene, including a sequence homologous to the binding site of the transcription factor Sp1, which has been suggested to affect the regulation of other housekeeping genes that have been characterized. An examination of the amino acid sequence indicates that the RP2 protein is praline-rich and is composed of alternating alpha-helix and beta-sheet regions. RP2 is probably not integrated into a membrane structure in the cell as it does not appear to contain hydrophobic regions capable of spanning a membrane.


1Present address: Reproduction Laboratory. Building 200, Beltsville Agricultural Research Center, Beltsville, MD 20705, USA

2Present address: Department of Biology, Yale University, New Haven, CT 06511, USA


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
EndocrinologyHome page
O. Levillain, J.-J. Diaz, O. Blanchard, and H. Dechaud
Testosterone Down-Regulates Ornithine Aminotransferase Gene and Up-Regulates Arginase II and Ornithine Decarboxylase Genes for Polyamines Synthesis in the Murine Kidney
Endocrinology, February 1, 2005; 146(2): 950 - 959.
[Abstract] [Full Text] [PDF]



Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.