Skip Navigation

This Article
Right arrow Print PDF (2667K)
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 (56)
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Sherman, L.
Right arrow Articles by Groner, Y.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Sherman, L.
Right arrow Articles by Groner, Y.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1984, Vol. 12, No. 24 9349-9365
© 1984


MOLECULAR BIOLOGY

Human Cu/Zn superoxide dismutase gene: molecular characterization of its two mRNA species

Levana Sherman, Ditsa Levanon, Judy Lieman-Hurwitz, Naomi Dafni and Yoram Groner

Department of Virology, The Weizmann Institute of Science Rehovot, 76100 Israel

Received September 18, 1984. Revised November 30, 1984. Accepted November 30, 1984.

Two cytoplasmic superoxide dismutase (SOD-1) mRNAs of about 0.7 and 0.9 kilobases (Kb.) were previously found in a variety of human cells. The two SOD-1 mRNAs are transcribed from the same gene and the major 0.7 Kb. species is approximately four times more abundant than the minor 0.9 Kb. mRNA. These two mRNAs differ in the length of their 3'-untranslated region and both have multiple 5'-ends. The longer transcript contains 222 additional nucleotides beyond the 3'-polyadenylated terminus of the short mRNA. S1 nuclease mapping and sequence analysis showed that these extra 222 nucleotides are specified by sequences contiguous to those shared by the two SOD-1 mRNAs. The 5'-termini of the two SOD-1 mRNAs were identified and mapped by both primer extension and S1 mapping. The majority of SOD-1 mRNA molecules (90–95%) have a 5'-start site located 23 base pairs (b.p.) downstream of the hexanucleotide -TATAAA-. The rest of the SOD-1 mRNA molecules have 5'-termini 30, 50 and 65 b.p. upstream from the major start region.


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
Am. J. Respir. Crit. Care Med.Home page
V. L. Kinnula and J. D. Crapo
Superoxide Dismutases in the Lung and Human Lung Diseases
Am. J. Respir. Crit. Care Med., June 15, 2003; 167(12): 1600 - 1619.
[Abstract] [Full Text] [PDF]


Home page
Biol. Reprod.Home page
J. D. Powell, R. Elshtein, D. J. Forest, and M. A. Palladino
Stimulation of Hypoxia-Inducible Factor-1 Alpha (HIF-1{alpha}) Protein in the Adult Rat Testis Following Ischemic Injury Occurs Without an Increase in HIF-1{alpha} Messenger RNA Expression
Biol Reprod, September 1, 2002; 67(3): 995 - 1002.
[Abstract] [Full Text] [PDF]


Home page
Cancer Res.Home page
A. Ravid, D. Rocker, A. Machlenkin, C. Rotem, A. Hochman, G. Kessler-Icekson, U. A. Liberman, and R. Koren
1,25-Dihydroxyvitamin D3 Enhances the Susceptibility of Breast Cancer Cells to Doxorubicin-induced Oxidative Damage
Cancer Res., February 1, 1999; 59(4): 862 - 867.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
W. Gu, C. Morales, and N. B. Hecht
In Male Mouse Germ Cells, Copper-Zinc Superoxide Dismutase Utilizes Alternative Promoters That Produce Multiple Transcripts with Different Translation Potential
J. Biol. Chem., January 6, 1995; 270(1): 236 - 243.
[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.