Regional mapping of a liver α-subunit gene of phosphorylase kinase (PHKA) to the distal region of human chromosome Xp

1992 ◽  
Vol 60 (3-4) ◽  
pp. 194-196 ◽  
Author(s):  
J.G. Wauters ◽  
P.J. Bossuyt ◽  
J. Davidson ◽  
J. Hendrickx ◽  
M.W. Kilimann ◽  
...  
Keyword(s):  
Human Chromosome ◽  
Distal Region ◽  
Alpha Subunit ◽  
Phosphorylase Kinase ◽  
Regional Mapping ◽  
Subunit Gene

Mapping of the phosphorylase kinase alpha subunit gene on the mouse X chromosome

1990 ◽  
Vol 53 (2-3) ◽  
pp. 91-94 ◽  
Author(s):  
P.J. Barnard ◽  
J.M.J. Derry ◽  
A.S. Ryder-Cook ◽  
N.F. Zander ◽  
M.W. Kilimann
Keyword(s):  
X Chromosome ◽  
Alpha Subunit ◽  
Phosphorylase Kinase ◽  
Subunit Gene

scholarly journals The chorionic gonadotropin alpha-subunit gene is on human chromosome 18 in JEG cells.

1983 ◽  
Vol 80 (20) ◽  
pp. 6282-6285 ◽  
Author(s):  
J. W. Hardin ◽  
M. E. Riser ◽  
J. M. Trent ◽  
P. O. Kohler
Keyword(s):  
Human Chromosome ◽  
Chorionic Gonadotropin ◽  
Alpha Subunit ◽  
Subunit Gene ◽  
Chromosome 18

scholarly journals A single gonadotropin alpha-subunit gene in normal tissue and tumor-derived cell lines.

1981 ◽  
Vol 256 (10) ◽  
pp. 5121-5127
Author(s):  
M. Boothby ◽  
R.W. Ruddon ◽  
C. Anderson ◽  
D. McWilliams ◽  
I. Boime
Keyword(s):  
Cell Lines ◽  
Normal Tissue ◽  
Alpha Subunit ◽  
Subunit Gene

scholarly journals Members of the Gq alpha subunit gene family activate phospholipase C beta isozymes.

1992 ◽  
Vol 267 (23) ◽  
pp. 16044-16047 ◽  
Author(s):  
C.H. Lee ◽  
D Park ◽  
D Wu ◽  
S.G. Rhee ◽  
M.I. Simon
Keyword(s):  
Gene Family ◽  
Phospholipase C ◽  
Alpha Subunit ◽  
Subunit Gene

A BgIII polymorphism at the ovine phosphorylase kinase alpha subunit locus (PHKA1)

2009 ◽  
Vol 25 (4) ◽  
pp. 288-288 ◽  
Author(s):  
M D Potts ◽  
V Hanrahan ◽  
D F Hill
Keyword(s):  
Alpha Subunit ◽  
Phosphorylase Kinase

scholarly journals The substrate specificity of adenosine 3′:5′-cyclic monophosphate-dependent protein kinase of rabbit skeletal muscle

1977 ◽  
Vol 162 (2) ◽  
pp. 411-421 ◽  
Author(s):  
S J Yeaman ◽  
P Cohen ◽  
D C Watson ◽  
G H Dixon
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Protein Kinase ◽  
Phosphorylation Site ◽  
Amino Acid Sequences ◽  
Beta Subunit ◽  
Alpha Subunit ◽  
Phosphorylase Kinase ◽  
Dependent Protein Kinase ◽  
Dependent Protein

The known amino acid sequences at the two sites on phosphorylase kinase that are phosphorylated by cyclic AMP-dependent protein kinase were extended. The sequences of 42 amino acids around the phosphorylation site on the alpha-subunit and of 14 amino acids around the phosphorylation site on the beta-subunit were shown to be: alpha-subunit Phe-Arg-Arg-Leu-Ser(P)-Ile-Ser-Thr-Glu-Ser-Glx-Pro-Asx-Gly-Gly-His-Ser-Leu-Gly-Ala-Asp-Leu-Met-Ser-Pro-Ser-Phe-Leu-Ser-Pro-Gly-Thr-Ser-Val-Phe(Ser,Pro,Gly)His-Thr-Ser-Lys; beta-subunit, Ala-Arg-Thr-Lys-Arg-Ser-Gly-Ser(P)-VALIle-Tyr-Glu-Pro-Leu-Lys. The sites on histone H2B which are phosphorylated by cyclic AMP-dependent protein kinase in vitro were identified as serine-36 and serine-32. The amino acid sequence in this region is: Lys-Lys-Arg-Lys-Arg-Ser32(P)-Arg-Lys-Glu-Ser36(P)-Tyr-Ser-Val-Tyr-Val- [Iwai, K., Ishikawa, K. & Hayashi, H. (1970) Nature (London) 226, 1056-1058]. Serine-36 was phosphorylated at 50% of the rate at which the beta-subunit of phosphorylase kinase was phosphorylated, and it was phosphorylated 6-7-fold more rapidly than was serine-32. The amino acid sequences when compared with those at the phosphorylation sites of other physiological substrates suggest that the presence of two adjacent basic amino acids on the N-terminal side of the susceptible serine residue may be critical for specific substrate recognition in vivo.

scholarly journals Rice OASA1D, a mutant anthranilate synthase .ALPHA. subunit gene, is an effective selectable marker for transformation of Arabidopsis thaliana

2005 ◽  
Vol 22 (4) ◽  
pp. 271-276 ◽  
Author(s):  
Makiko Kawagishi-Kobayashi ◽  
Naoto Yabe ◽  
Mizuho Tsuchiya ◽  
Sachiyo Harada ◽  
Tomoko Kobayashi ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Selectable Marker ◽  
Alpha Subunit ◽  
Anthranilate Synthase ◽  
Subunit Gene

Expression of the glycoprotein hormone alpha-subunit gene in the placenta requires a functional cyclic AMP response element, whereas a different cis-acting element mediates pituitary-specific expression

1989 ◽  
Vol 9 (11) ◽  
pp. 5113-5122
Author(s):  
J A Bokar ◽  
R A Keri ◽  
T A Farmerie ◽  
R A Fenstermaker ◽  
B Andersen ◽  
...  
Keyword(s):  
Cyclic Amp ◽  
Transgenic Mice ◽  
Regulatory Region ◽  
Alpha Subunit ◽  
Subunit Gene ◽  
Glycoprotein Hormone ◽  
Specific Expression ◽  
Response Element ◽  
Cyclic Amp Response Element ◽  
Choriocarcinoma Cells

The single-copy gene encoding the alpha subunit of glycoprotein hormones is expressed in the pituitaries of all mammals and in the placentas of only primates and horses. We have systematically analyzed the promoter-regulatory elements of the human and bovine alpha-subunit genes to elucidate the molecular mechanisms underlying their divergent patterns of tissue-specific expression. This analysis entailed the use of transient expression assays in a chorionic gonadotropin-secreting human choriocarcinoma cell line, protein-DNA binding assays, and expression of chimeric forms of human or bovine alpha subunit genes in transgenic mice. From the results, we conclude that placental expression of the human alpha-subunit gene requires a functional cyclic AMP response element (CRE) that is present as a tandem repeat in the promoter-regulatory region. In contrast, the promoter-regulatory region of the bovine alpha-subunit gene, as well as of the rat and mouse genes, was found to contain a single CRE homolog that differed from its human counterpart by a single nucleotide. This difference substantially reduced the binding affinity of the bovine CRE homolog for the nuclear protein that bound to the human alpha CRE and thereby rendered the bovine alpha-subunit promoter inactive in human choriocarcinoma cells. However, conversion of the bovine alpha CRE homolog to an authentic alpha CRE restored activity to the bovine alpha-subunit promoter in choriocarcinoma cells. Similarly, a human but not a bovine alpha transgene was expressed in placenta in transgenic mice. Thus, placenta-specific expression of the human alpha-subunit gene may be the consequence of the recent evolution of a functional CRE. Expression of the human alpha transgene in mouse placenta further suggests that evolution of placenta-specific trans-acting factors preceded the appearance of this element. Finally, in contrast to their divergent patterns of placental expression, both the human and bovine alpha-subunit transgenes were expressed in mouse pituitary, indicating differences in the composition of the enhancers required for pituitary- and placenta-specific expression.

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