Similarities between legume–rhizobium communication and steroid-mediated intercellular communication in vertebrates

1992 ◽  
Vol 38 (6) ◽  
pp. 541-547 ◽  
Author(s):  
Michael E. Baker
Keyword(s):  
Nitrogen Fixation ◽  
Biological Activity ◽  
Amino Acid ◽  
Bradyrhizobium Japonicum ◽  
Common Ancestor ◽  
Rhizobium Meliloti ◽  
Hydroxysteroid Dehydrogenase ◽  
Nod Factors ◽  
Sequence Analyses ◽  
Metabolizing Enzymes

Regulation of the actions of flavonoids and Nod factors in legume–rhizobia communication has several interesting similarities with that of steroid-mediated actions in vertebrates. Oxidation or reduction of flavonoids and Nod factors modifies their biological activity just as, for example, oxidation of an alcohol at C11 on hydrocortisone regulates its biological activity. Second, some flavonoids are anti-inducers, functioning like steroid antagonists to negate the actions of inducer flavonoids. Amino acid sequence analyses show that human 17β-hydroxysteroid dehydrogenase, which catalyzes the interconversion of the alcohol and ketone at C17 on estrogens and androgens, and rat 11β-hydroxysteroid dehydrogenase, which catalyzes the interconversion of the alcohol and ketone at C11 of glucocorticoids, and Rhizobium meliloti NodG and Bradyrhizobium japonicum. FixR are derived from a common ancestor. Just as steroid-metabolizing enzymes can regulate steroid-mediated gene transcription, enzymes that modify substituents on flavonoids and Nod factors may have a similar role in regulating signalling between legumes and rhizobia. The enzymes that modify flavonoids and Nod factors have not yet been identified. However, NodG and FixR are two likely candidates to have this role in regulating legume–rhizobia signalling. Key words: NodG function, FixR function, steroid–flavonoid similarities, steroids and nitrogen fixation.

scholarly journals Going Forward and Back: The Complex Evolutionary History of the GPx

Biology ◽  
2021 ◽  
Vol 10 (11) ◽  
pp. 1165
Author(s):  
Thomaz Stumpf Trenz ◽  
Camila Luiza Delaix ◽  
Andreia Carina Turchetto-Zolet ◽  
Marcel Zamocky ◽  
Fernanda Lazzarotto ◽  
...  
Keyword(s):  
Amino Acid ◽  
Glutathione Peroxidase ◽  
Phylogenetic Trees ◽  
Evolutionary History ◽  
Common Ancestor ◽  
Sequence Analyses ◽  
History Of ◽  
Substrate Usage ◽  
Encoding Genes ◽  
Complex Evolutionary History

There is large diversity among glutathione peroxidase (GPx) enzymes regarding their function, structure, presence of the highly reactive selenocysteine (SeCys) residue, substrate usage, and reducing agent preference. Moreover, most vertebrate GPxs are very distinct from non-animal GPxs, and it is still unclear if they came from a common GPx ancestor. In this study, we aimed to unveil how GPx evolved throughout different phyla. Based on our phylogenetic trees and sequence analyses, we propose that all GPx encoding genes share a monomeric common ancestor and that the SeCys amino acid was incorporated early in the evolution of the metazoan kingdom. In addition, classical GPx and the cysteine-exclusive GPx07 have been present since non-bilaterian animals, but they seem to have been lost throughout evolution in different phyla. Therefore, the birth-and-death of GPx family members (like in other oxidoreductase families) seems to be an ongoing process, occurring independently across different kingdoms and phyla.

Synthesis of β-glucans by Bradyrhizobium japonicum and Rhizobium fredii

1992 ◽  
Vol 38 (6) ◽  
pp. 510-514 ◽  
Author(s):  
Arvind A. Bhagwat ◽  
Donald L. Keister
Keyword(s):  
Molecular Weight ◽  
Nitrogen Fixation ◽  
Membrane Protein ◽  
Bradyrhizobium Japonicum ◽  
Rhizobium Meliloti ◽  
Uridine Diphosphate ◽  
Enzyme Preparations ◽  
Rhizobium Fredii ◽  
Diphosphate Glucose

Particulate enzyme preparations from Rhizobium and Bradyrhizobium synthesize β-glucans when incubated with uridine diphosphate glucose (UDP-glucose) and a divalent cation. Synthesis of β-1,2-linked glucans in Rhizobium fredii involves the product of the ndvB gene, a 319-kDa membrane protein, which is labeled with [14C]glucose from UDP-[14C]glucose as previously demonstrated in Rhizobium meliloti and Agrobacterium sp. Bradyrhizobium japonicum synthesize β-1,3- and β-1,6-linked glucans of a lower molecular weight than those synthesized by R. meliloti. In comparative experiments, no evidence was found for a protein-bound intermediate in B. japonicum. The ndvB gene of R. fredii was mobilized to B. japonicum and the gene was expressed, as evidenced by appearance of a large membrane protein (ca. 319 kDa) which was labeled with UDP-[14C]glucose in vitro. Key words: soybean, nitrogen fixation, β-glucan, Bradyrhizobium, Rhizobium.

Biological Function and Chemistry of Endothelin. A Review

1999 ◽  
Vol 64 (8) ◽  
pp. 1211-1252 ◽  
Author(s):  
Jan Hlaváček ◽  
Renáta Marcová
Keyword(s):  
Biological Activity ◽  
Amino Acid ◽  
Biological Function ◽  
Biological Properties ◽  
Structural Basis ◽  
Amino Acid Residues ◽  
Snake Venoms ◽  
Vasoactive Peptides ◽  
Physico Chemical ◽  
Endothelin A

The first part of this review deals with the biosynthesis and a biological function of strongly vasoactive peptides named endothelins (ETs) including vasoactive intestinal contractor. Where it was useful, snake venoms sarafotoxins which are structural endothelin derivatives, were also mentioned. In the second part, an attention is paid to structural basis of the ETs biological activity, with respect to alterations of amino acid residues in the parent peptides modifying the conformation and consequently the physico-chemical and biological properties in corresponding ETs analogs. Special attention is focussed on the area of ETs receptors and their interaction with peptide and non peptide agonists and antagonists, important in designing selective inhibitors of ETs receptors potentially applicable as drugs in a medicine. A review with 182 references.

EFFECTS OF SOIL ACIDITY ON RHIZOBIA NUMBERS, NODULATION AND NITROGEN FIXATION BY ALFALFA AND RED CLOVER

1977 ◽  
Vol 57 (2) ◽  
pp. 197-203 ◽  
Author(s):  
W. A. RICE ◽  
D. C. PENNEY ◽  
M. NYBORG
Keyword(s):  
Nitrogen Fixation ◽  
Soil Ph ◽  
Soil Acidity ◽  
Field Experiments ◽  
Rhizobium Meliloti ◽  
Acid Soils ◽  
Red Clover ◽  
Ion Concentration ◽  
Hydrogen Ion Concentration ◽  
Greenhouse Experiments

The effects of soil acidity on nitrogen fixation by alfalfa (Medicago sativa L.) and red clover (Trifolium pratense L.) were investigated in field experiments at 28 locations, and in greenhouse experiments using soils from these locations. The pH of the soils (limed and unlimed) varied from 4.5 to 7.2. Rhizobia populations in the soil, nodulation, and relative forage yields (yield without N/yield with N) were measured in both the field and greenhouse experiments. Rhizobium meliloti numbers, nodulation scores, and relative yields of alfalfa decreased sharply as the pH of the soils decreased below 6.0. For soils with pH 6.0 or greater, there was very little effect of pH on any of the above factors for alfalfa. Soil pH in the range studied had no effect on nodulation scores and relative yields of red clover. However, R. trifolii numbers were reduced when the pH of the soil was less than 4.9. These results demonstrate that hydrogen ion concentration is an important factor limiting alfalfa growth on acid soils of Alberta and northeastern British Columbia, but it is less important for red clover. This supports the continued use of measurements of soil pH, as well as plant-available Al and Mn for predicting crop response to lime.

scholarly journals Transcriptional Response of Soybean Suspension-cultured Cells Induced by Nod Factors Obtained from Bradyrhizobium japonicum USDA110

2002 ◽  
Vol 43 (11) ◽  
pp. 1314-1322
Author(s):  
Tsuneo Hakoyama ◽  
Tadashi Yokoyama ◽  
Hiroshi Kouchi ◽  
Ken-ichi Tsuchiya ◽  
Hisatoshi Kaku ◽  
...  
Keyword(s):  
Bradyrhizobium Japonicum ◽  
Cultured Cells ◽  
Transcriptional Response ◽  
Nod Factors ◽  
Suspension Cultured Cells

scholarly journals Transforming growth factor alpha: mutation of aspartic acid 47 and leucine 48 results in different biological activities.

1988 ◽  
Vol 8 (3) ◽  
pp. 1247-1252 ◽  
Author(s):  
E Lazar ◽  
S Watanabe ◽  
S Dalton ◽  
M B Sporn
Keyword(s):  
Amino Acids ◽  
Biological Activity ◽  
Amino Acid ◽  
Growth Factor ◽  
Aspartic Acid ◽  
Transforming Growth Factor ◽  
Biologically Active ◽  
Single Amino Acid ◽  
Transforming Growth Factor Alpha ◽  
Factor Alpha

To study the relationship between the primary structure of transforming growth factor alpha (TGF-alpha) and some of its functional properties (competition with epidermal growth factor (EGF) for binding to the EGF receptor and induction of anchorage-independent growth), we introduced single amino acid mutations into the sequence for the fully processed, 50-amino-acid human TGF-alpha. The wild-type and mutant proteins were expressed in a vector by using a yeast alpha mating pheromone promoter. Mutations of two amino acids that are conserved in the family of the EGF-like peptides and are located in the carboxy-terminal part of TGF-alpha resulted in different biological effects. When aspartic acid 47 was mutated to alanine or asparagine, biological activity was retained; in contrast, substitutions of this residue with serine or glutamic acid generated mutants with reduced binding and colony-forming capacities. When leucine 48 was mutated to alanine, a complete loss of binding and colony-forming abilities resulted; mutation of leucine 48 to isoleucine or methionine resulted in very low activities. Our data suggest that these two adjacent conserved amino acids in positions 47 and 48 play different roles in defining the structure and/or biological activity of TGF-alpha and that the carboxy terminus of TGF-alpha is involved in interactions with cellular TGF-alpha receptors. The side chain of leucine 48 appears to be crucial either indirectly in determining the biologically active conformation of TGF-alpha or directly in the molecular recognition of TGF-alpha by its receptor.

“In vivo” amplification of biological activity of tetragastrin by amino acid hydroxamates

1984 ◽  
Vol 4 (12) ◽  
pp. 1009-1015 ◽  
Author(s):  
J. P. Bali ◽  
H. Mattras ◽  
A. Previero ◽  
M. A. Coletti-Previero
Keyword(s):  
Biological Activity ◽  
Amino Acid ◽  
Aromatic Amino Acid ◽  
Aminopeptidase Activity ◽  
Proteolytic Degradation ◽  
Short Peptides ◽  
Rat Blood ◽  
Active Peptides

Rat blood was shown to contain an aminopeptidase which rapidly hydrolyses short peptides containing an aromatic amino acid as N-terminal residue. Using tetragastrin (Trp-Met-Asp-PheNH 2) as substrate, we showed that some amino acid hydroxamates inhibit rat aminopeptidase activity ‘in vitro’ in the following order: HTrpNHOH > HPheNHOH ≫ HAIaNHOH. The same hydroxamates markedly enhanced the biological activity of tetragastrin ‘in vivo’. The amplification of the secretory effect, correlated with the amount of the hydroxamate used, strongly suggests that these compounds can stabilize a number of active peptides in vivo by inhibiting their proteolytic degradation.

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