TY - JOUR
T1 - Isolation and Characterization of the Human Tyrosine Hydroxylase Gene
T2 - Identification of 5’ Alternative Splice Sites Responsible for Multiple mRNAs
AU - O’Malley, Karen L.
AU - Anhalt, Michael J.
AU - Martin, Brian M.
AU - Kelsoe, John R.
AU - Winfield, Susan L.
AU - Ginns, Edward I.
PY - 1987
Y1 - 1987
N2 - A full-length genomic clone for human tyrosine hydroxylase (L-tyrosine, tetrahydropteridine:oxygen oxidoreductase, EC 1.14.16.2) has been isolated. A human brain genomic library constructed in EMBL3 was screened by using a rat cDNA for tyrosine hydroxylase as a probe [Brown, E. R., Coker, G. T., III, & O’Malley, K. L. (1987) Biochemistry 26, 5208–5212]. Out of one million recombinant phage, one clone was identified that hybridized to both 5’ and 3’ rat cDNA probes. Restriction endonuclease mapping, Southern blotting, and sequence analysis revealed that, like its rodent counterpart, the human gene is single copy, contains 13 primary exons, and spans approximately 8 kilobases (kb). In contrast to the rat gene, human tyrosine hydroxylase undergoes alternative RNA processing within intron 1, generating at least three distinct mRNAs. A comparison of the human tyrosine hydroxylase and phenylalanine hydroxylase [DiLella, A. G., Kwok, S. C. M., Ledley, F. D., Marvit, J., & Woo, S. L. C. (1986) Biochemistry 25, 743–749] genes indicates that although both probably evolved from a common ancestral gene, major changes in the size of introns have occurred since their divergence.
AB - A full-length genomic clone for human tyrosine hydroxylase (L-tyrosine, tetrahydropteridine:oxygen oxidoreductase, EC 1.14.16.2) has been isolated. A human brain genomic library constructed in EMBL3 was screened by using a rat cDNA for tyrosine hydroxylase as a probe [Brown, E. R., Coker, G. T., III, & O’Malley, K. L. (1987) Biochemistry 26, 5208–5212]. Out of one million recombinant phage, one clone was identified that hybridized to both 5’ and 3’ rat cDNA probes. Restriction endonuclease mapping, Southern blotting, and sequence analysis revealed that, like its rodent counterpart, the human gene is single copy, contains 13 primary exons, and spans approximately 8 kilobases (kb). In contrast to the rat gene, human tyrosine hydroxylase undergoes alternative RNA processing within intron 1, generating at least three distinct mRNAs. A comparison of the human tyrosine hydroxylase and phenylalanine hydroxylase [DiLella, A. G., Kwok, S. C. M., Ledley, F. D., Marvit, J., & Woo, S. L. C. (1986) Biochemistry 25, 743–749] genes indicates that although both probably evolved from a common ancestral gene, major changes in the size of introns have occurred since their divergence.
UR - http://www.scopus.com/inward/record.url?scp=0023490535&partnerID=8YFLogxK
U2 - 10.1021/bi00396a007
DO - 10.1021/bi00396a007
M3 - Article
C2 - 2892528
AN - SCOPUS:0023490535
SN - 0006-2960
VL - 26
SP - 6910
EP - 6914
JO - Biochemistry
JF - Biochemistry
IS - 22
ER -