The follicle-stimulating hormone β-subunit gene of the common brushtail possum (Trichosurus vulpecula): analysis of cDNA sequence and expression

1997 ◽  
Vol 9 (8) ◽  
pp. 795 ◽  
Author(s):  
Stephen B. Lawrence ◽  
Dominique M. Vanmontfort ◽  
David J. Tisdall ◽  
Kenneth P. McNatty ◽  
Andrew E. Fidler

Reverse transcription–PCR has been used to obtain a cDNA sequence from the follicle-stimulating hormone (FSH) β-subunit gene of the Australian brushtail possum (Trichosurus vulpecula). Comparisons of the possum FSHβ-mRNA coding region nucleotide sequence with that of six eutherian mammal homologues reveals a mean percent identity of 77·3% and 76·8% at the nucleotide and predicted amino acid-sequence levels respectively. Furthermore, the predicted amino acid sequence of the possum FSHβ mature protein shows evolutionary conservation of twelve cysteine residues and two potential N-linked glycosylation sites. The protein lacks the CAGY motif present in most reported glycoprotein β-subunit sequences. The translation termination codon and consensus polyadenylation sequence overlap, a feature observed in other mammalian FSHβ genes. Northern hybridization of total RNA from adult female possum pituitary revealed three hybridizing transcripts of approximately 2·8, 1·2 and 0·5 kb which may arise from utilizing alternative polyadenylation signals. In situ hybridization localized the FSHβ transcripts to a sub-population of anterior pituitary cells interpreted as being gonadotropes. In summary the results indicate considerable evolutionary conservation of the structure of the FSH b-subunit gene between the marsupial and eutherian mammalian lineages.

1998 ◽  
Vol 10 (3) ◽  
pp. 289 ◽  
Author(s):  
Katherine Belov ◽  
Gavan A. Harrison ◽  
Desmond W. Cooper

The cDNA encoding the follicle stimulating hormone beta subunit (FSH-β) was isolated from a red kangaroo pituitary cDNA library by using a porcine probe and the nucleotide sequence for the coding region was determined. The highest degree of deduced amino acid sequence identity (91%) was observed between the red kangaroo and another marsupial, the brushtail possum (Trichosurus vulpecula), followed by eutherian species (76%, 75% and 74%, respectively, for pig, mouse and sheep). Based on the deduced red kangaroo FSH-β amino acid sequence, putative antigenic sites have been identified that may prove useful for studying the hormonal control of reproduction in marsupials.


1998 ◽  
Vol 250 (3) ◽  
pp. 664-667 ◽  
Author(s):  
Bronislava Črešnar ◽  
Andreja Plaper ◽  
Katja Breskvar ◽  
Tamara Hudnik-Plevnik

1988 ◽  
Vol 2 (9) ◽  
pp. 806-815 ◽  
Author(s):  
J. Larry Jameson ◽  
Carolyn B. Becker ◽  
Christine M. Lindell ◽  
Joel F. Habener

1992 ◽  
Vol 12 (2) ◽  
pp. 598-608
Author(s):  
J D Chen ◽  
C S Chan ◽  
V Pirrotta

The zeste gene product is involved in two types of genetic effects dependent on chromosome pairing: transvection and the zeste-white interaction. Comparison of the predicted amino acid sequence with that of the Drosophila virilis gene shows that several blocks of amino acid sequence have been very highly conserved. One of these regions corresponds to the DNA binding domain. Site-directed mutations in this region indicate that a sequence resembling that of the homeodomain DNA recognition helix is essential for DNA binding activity. The integrity of an amphipathic helical region is also essential for binding activity and is likely to be responsible for dimerization of the DNA binding domain. Another very strongly conserved domain of zeste is the C-terminal region, predicted to form a long helical structure with two sets of heptad repeats that constitute two long hydrophobic ridges at opposite ends and on opposite faces of the helix. We show that this domain is responsible for the extensive aggregation properties of zeste that are required for its role in transvection phenomena. A model is proposed according to which the hydrophobic ridges induce the formation of open-ended coiled-coil structures holding together many hundreds of zeste molecules and possibly anchoring these complexes to other nuclear structures.


1992 ◽  
Vol 263 (3) ◽  
pp. R489-R495 ◽  
Author(s):  
A. M. Pajor ◽  
B. A. Hirayama ◽  
E. M. Wright

The rabbit intestinal Na(+)-glucose cotransporter has been cloned and sequenced. The cDNA encoding the cotransporter has been used in two general lines of research related to comparative aspects of Na(+)-glucose cotransport that are reviewed here. First, defined regions of the predicted amino acid sequence were used to raise antibodies, and the species distribution of epitopes recognized by those antibodies was investigated. Intestinal brush-border membranes from mammals, birds, an amphibian, and a reptile were all found to contain protein that were recognized by the antibodies in Western analysis. The cDNA encoding the rabbit intestinal Na(+)-glucose cotransporter was also used directly to examine the species distribution of related mRNA in Northern studies and to isolate new cDNAs encoding other Na(+)-glucose cotransporters. Northern blots revealed the presence of related mRNAs in intestines of mammals and a fish, as well as rabbit kidney and gills of marine mussels. The cDNAs encoding mammalian Na(+)-glucose cotransporters and bacterial Na(+)-dependent cotransporters for proline and pantothenate share sequence homology. There has been evolutionary conservation of the structure and function of the Na(+)-glucose cotransporter, and there appears to be a gene family that codes for the Na(+)-coupled cotransporters.


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