Pike eel (Muraenesox cinereus) gonadotropin. Amino acid sequences of both alpha and beta subunits

Active transport across the vacuolar components of the eukaryotic endomembrane system is energized by a specific vacuolar H+-ATPase. The amino acid sequences of the 70- and 60-kDa subunits of the vacuolar H+-ATPase are approximately equal to 25% identical to the beta and alpha subunits, respectively, of the eubacterial-type F0F1-ATPases. We now report that the same vacuolar H+-ATPase subunits are approximately equal to 50% identical to the alpha and beta subunits, respectively, of the sulfur-metabolizing Sulfolobus acidocaldarius, an archaebacterium (Archaeobacterium). Moreover, the homologue of an 88-amino acid stretch near the amino-terminal end of the 70-kDa subunit is absent from the F0F1-ATPase beta subunit but is present in the alpha subunit of Sulfolobus. Since the two types of subunits (alpha and beta subunits; 60- and 70-kDa subunits) are homologous to each other, they must have arisen by a gene duplication that occurred prior to the last common ancestor of the eubacteria, eukaryotes, and Sulfolobus. Thus, the phylogenetic tree of the subunits can be rooted at the site where the gene duplication occurred. The inferred evolutionary tree contains two main branches: a eubacterial branch and an eocyte branch that gave rise to Sulfolobus and the eukaryotic host cell. The implication is that the vacuolar H+-ATPase of eukaryotes arose by the internalization of the plasma membrane H+-ATPase of an archaebacterial-like ancestral cell.

Download Full-text

Structural heterogeneity of Pseudomonas aeruginosa bacterioferritin

Biochemical Journal ◽

10.1042/bj3040493 ◽

1994 ◽

Vol 304 (2) ◽

pp. 493-497 ◽

Cited By ~ 30

Author(s):

G R Moore ◽

F H Kadir ◽

F K al-Massad ◽

N E Le Brun ◽

A J Thomson ◽

...

Keyword(s):

Amino Acids ◽

Pseudomonas Aeruginosa ◽

Amino Acid ◽

Amino Acid Sequence ◽

Structural Heterogeneity ◽

Amino Acid Sequences ◽

Binding Study ◽

Alpha Subunit ◽

Beta Subunits ◽

Binding Characteristics

The subunit composition, amino acid sequence and haem-binding characteristics of bacterioferritin (BFR) from Pseudomonas aeruginosa have been studied. Unlike other BFRs, P. aeruginosa BFR was found to contain two subunit types, designated alpha and beta, which differed considerably in their amino acid sequences. The N-terminal 69 and 55 amino acids of the alpha and beta subunits respectively were determined. The alpha subunit differed most from other BFRs. The two subunits were present in variable proportions in different preparations. The maximum stoichiometry of haem binding was found to be sample-dependent and to be different from the previously reported one per subunit [Kadir and Moore (1990) FEBS Lett. 271, 141-143]. This previous haem-binding study was shown to have been carried out with damaged protein, which contained both normal alpha and beta subunits and shorter versions of these that appeared to have been produced by cleavage of the normal subunits. The possibility that aging processes degrade ferritins and affect their haem-binding characteristics is discussed.

Download Full-text

Primary structure of allophycocyanin from the unicellular rhodophyte, Cyanidium caldarium. The complete amino acid sequences of the alpha and beta subunits.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)44587-x ◽

1983 ◽

Vol 258 (16) ◽

pp. 9931-9940 ◽

Cited By ~ 3

Author(s):

G D Offner ◽

R F Troxler

Keyword(s):

Amino Acid ◽

Primary Structure ◽

Amino Acid Sequences ◽

Beta Subunits ◽

Cyanidium Caldarium

Download Full-text

Phycobilin-apoprotein linkages in the alpha and beta subunits of phycocyanin from the unicellular rhodophyte, Cyanidium caldarium. Amino acid sequences of 35S-labeled chromopeptides.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)36018-6 ◽

1979 ◽

Vol 254 (16) ◽

pp. 7803-7811 ◽

Cited By ~ 4

Author(s):

A.S. Brown ◽

G.D. Offner ◽

M.M. Ehrhardt ◽

R.F. Troxler

Keyword(s):

Amino Acid ◽

Amino Acid Sequences ◽

Beta Subunits ◽

Cyanidium Caldarium

Download Full-text

Blue gourami (Trichogaster trichopterus) gonadotropic beta subunits (I and II) cDNA sequences and expression during oogenesis

Journal of Molecular Endocrinology ◽

10.1677/jme.0.0230177 ◽

1999 ◽

Vol 23 (2) ◽

pp. 177-187 ◽

Cited By ~ 53

Author(s):

K Jackson ◽

D Goldberg ◽

M Ofir ◽

M Abraham ◽

G Degani

Keyword(s):

Amino Acid ◽

Sequence Analysis ◽

Pituitary Gland ◽

Oocyte Maturation ◽

Striped Bass ◽

Reproductive Cycle ◽

Amino Acid Sequences ◽

Beta Subunits ◽

Cdna Sequences

We have cloned two cDNAs from the pituitary gland of blue gourami (Trichogaster trichopterus), coding for the beta subunits of the gonadotropin hormones GtH-I and GtH-II. The two cDNAs were sequenced and subjected to sequence analysis. We have found that the deduced amino acid sequences of both cDNAs were most similar to their striped bass counterparts. The beta GtH-I subunits of blue gourami and striped bass shared 73% of their residues, and the beta GtH-II subunits 84%.The cloning of the cDNAs of beta GtH-I and beta GtH-II has enabled us to measure the expression of their respective mRNAs in the pituitaries of female blue gourami at different stages of the reproductive cycle. The highest levels of beta GtH-I and beta GtH-II mRNA were found in specimens classified as high vitellogenic and in females that were at the final stages of oocyte maturation.

Download Full-text

A comprehensive evolutionary analysis based on nucleotide and amino acid sequences of the alpha- and beta-subunits of glycoprotein hormone gene family

Journal of Endocrinology ◽

10.1677/joe.0.1560529 ◽

1998 ◽

Vol 156 (3) ◽

pp. 529-542 ◽

Cited By ~ 112

Author(s):

MD Li ◽

JJ Ford

Keyword(s):

Amino Acid ◽

Phylogenetic Trees ◽

Evolutionary History ◽

Amino Acid Sequences ◽

Bony Fish ◽

Beta Subunit ◽

Beta Subunits ◽

Type I ◽

Evolutionary Analysis ◽

Glycoprotein Hormone

On the basis of nucleotide sequences of the coding region and their predicted amino acid sequences, 58 glycoprotein hormone subunit genes were compared, aligned and used to construct phylogenetic trees for this family. The analysis included 17 alpha-subunits, eight TSH beta-, six FSH beta-, 17 LH beta/CG beta-, four fish gonadotropin (GTH)-I beta-, five fish GTH-II beta- and one additional fish GTH beta-subunit. The reliability of the phylogenetic trees was probed with the bootstrapping test. Our results indicated that: both the alpha- and beta-subunits of the family diverged from a common ancestral gene about 927 million years ago, the initial precursor of the beta-subunit duplicated to give rise to the LH beta and a second hormone, the latter then duplicating to FSH beta and TSH beta, so that FSH beta is related more to TSH beta than to LH beta; and bony fish GTH-I beta is highly related to mammalian FSH beta, whereas the bony fish GTH-II beta is more related to mammalian LH beta. For scientific consistency and convenience, we propose that the following nomenclature be adopted, all fish gonadotropins of type I be classified as FSH and all type II be classified as LH hormones. In addition, on the basis of results from this and other studies, we propose an evolutionary history for this glycoprotein hormone family. Reconstruction of the evolutionary history of this family would not only provide clues to understanding thyrotropin and gonadotropin functions, but would also allow further revision of the present nomenclature of the gonadotropins in fish.

Download Full-text