Leghemoglobin variability in the genus Phaseolus

1991 ◽  
Vol 69 (2) ◽  
pp. 353-358 ◽  
Author(s):  
M. M. Lülsdorf ◽  
F. B. Holl
Keyword(s):  
Interspecific Hybrids ◽  
Root Nodule ◽  
Structural Heterogeneity ◽  
Phaseolus Lunatus ◽  
Oxygen Binding ◽  
Amino Terminal ◽  
Key Words Nitrogen Fixation ◽  
Terminal Amino ◽  
Phaseolus Species ◽  
Key Words Nitrogen

Leghemoglobins are oxygen-binding proteins in the legume root nodule that generally show structural heterogeneity. Fifty accessions of the genus Phaseolus were screened for leghemoglobin electrophoretic variation. Heterogeneity was observed in two of the six Phaseolus species investigated; the single leghemoglobin components found in samples of Phaseolus vulgaris and Phaseolus acutifolius nodule extracts, as well as in other Phaseolus species, appear to be the exception among nitrogen-fixing plants that have been evaluated for leghemoglobin profiles. Interspecific hybrids were produced to transfer existing leghemoglobin variability into the P. vulgaris background. Leghemoglobins were also shown to be inherited codominantly in interspecific hybrids. The amino terminal amino acid sequence of leghemoglobin II of a P. vulgaris × Phaseolus filiformis hybrid and leghemoglobins I and II from Phaseolus lunatus nodules were determined. The 37 amino terminal amino acids of these components were identical to the published sequence for P. vulgaris. Key words: nitrogen fixation, interspecific hybrids, electrophoresis.

N-Terminal amino acid sequence of rat tonin: homology with serine proteases

1978 ◽  
Vol 56 (9) ◽  
pp. 920-925 ◽  
Author(s):  
N. G. Seidah ◽  
R. Routhier ◽  
M. Caron ◽  
M. Chrétien ◽  
S. Demassieux ◽  
...  
Keyword(s):  
Serine Proteases ◽  
Terminal Sequence ◽  
Renin Substrate ◽  
Amino Terminal ◽  
Single Polypeptide Chain ◽  
Serine Protease Family ◽  
Terminal Amino ◽  
Single Polypeptide ◽  
Carboxy Terminal ◽  
Amino Terminal Sequence

In this paper, we present the amino-terminal sequence of rat tonin, an endopeptidase responsible for the conversion of angiotensinogen, the tetradecapeptide renin substrate, or angiotensin I to angiotensin II. It is shown that isoleucine and proline occupy the amino- and carboxy-terminal residues respectively. The N-terminal sequence analysis permitted the identification of 34 out of the first 40 residue s of the single polypeptide chain composed of 272 amino acids. The se results showed an extensive homology with the sequence of many serine proteases of the trypsin–chymotrypsin family. This information, coupled with the slow inhibition of tonin by diisopropylfluorophosphate, classified this enzyme as a selective endopeptidase of the active serine protease family.

scholarly journals Specificity of RNA Binding by CPEB: Requirement for RNA Recognition Motifs and a Novel Zinc Finger

1998 ◽  
Vol 18 (2) ◽  
pp. 685-693 ◽  
Author(s):  
Laura E. Hake ◽  
Raul Mendez ◽  
Joel D. Richter
Keyword(s):  
Zinc Finger ◽  
Rna Binding ◽  
Rna Recognition ◽  
Cytoplasmic Polyadenylation ◽  
Functional Motif ◽  
Rna Recognition Motifs ◽  
Amino Terminal ◽  
Terminal Amino ◽  
Maternal Mrnas ◽  
Recognition Motifs

ABSTRACT CPEB is an RNA binding protein that interacts with the maturation-type cytoplasmic polyadenylation element (CPE) (consensus UUUUUAU) to promote polyadenylation and translational activation of maternal mRNAs in Xenopus laevis. CPEB, which is conserved from mammals to invertebrates, is composed of three regions: an amino-terminal portion with no obvious functional motif, two RNA recognition motifs (RRMs), and a cysteine-histidine region that is reminiscent of a zinc finger. In this study, we investigated the physical properties of CPEB required for RNA binding. CPEB can interact with RNA as a monomer, and phosphorylation, which modifies the protein during oocyte maturation, has little effect on RNA binding. Deletion mutations of CPEB have been overexpressed inEscherichia coli and used in a series of RNA gel shift experiments. Although a full-length and a truncated CPEB that lacks 139 amino-terminal amino acids bind CPE-containing RNA avidly, proteins that have had either RRM deleted bind RNA much less efficiently. CPEB that has had the cysteine-histidine region deleted has no detectable capacity to bind RNA. Single alanine substitutions of specific cysteine or histidine residues within this region also abolish RNA binding, pointing to the importance of this highly conserved domain of the protein. Chelation of metal ions by 1,10-phenanthroline inhibits the ability of CPEB to bind RNA; however, RNA binding is restored if the reaction is supplemented with zinc. CPEB also binds other metals such as cobalt and cadmium, but these destroy RNA binding. These data indicate that the RRMs and a zinc finger region of CPEB are essential for RNA binding.

scholarly journals THE AMINO-TERMINAL AMINO ACIDS OF PAROTIN

1960 ◽  
Vol 7 (3) ◽  
pp. 175-180
Author(s):  
YUKIHO KUBOTA
Keyword(s):  
Amino Acids ◽  
Amino Terminal ◽  
Terminal Amino

Neisseria pili proteins: amino-terminal amino acid sequences and identification of an unusual amino acid

Biochemistry ◽  
1978 ◽  
Vol 17 (3) ◽  
pp. 442-445 ◽  
Author(s):  
Mark A. Hermodson ◽  
Kirk C. S. Chen ◽  
Thomas M. Buchanan
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequences ◽  
Terminal Amino Acid ◽  
Amino Terminal ◽  
Terminal Amino ◽  
Unusual Amino Acid

Inhibition of renin release from rat kidney slices by the angiotensins

1978 ◽  
Vol 235 (1) ◽  
pp. F62-F68 ◽  
Author(s):  
A. J. Naftilan ◽  
S. Oparil
Keyword(s):  
Direct Action ◽  
Rat Kidney ◽  
Sharp Decrease ◽  
Renin Release ◽  
Structural Basis ◽  
Response Curves ◽  
Amino Terminal ◽  
Kidney Slices ◽  
Angiotensin Iii ◽  
Terminal Amino

The mechanism and structural basis of the inhibition of renin release by angiotensin II (AII) were studied in rat kidney slices. Renin release was inhibited by AII and the (2–8), (3–8), (4–8), and (5–8) peptides of AII (5 X 10(-5) M). These constituent peptides of AII which share a common carboxyl terminus inhibited renin release with a sharp decrease in potency when the amino-terminal amino acid was removed. Saralasin attenuated the inhibition of renin release induced by equimolar concentrations of AII. Dose-response curves for AII and the (2–8) peptide [angiotensin III (AIII)] indicate that AII is a more potent inhibitor of renin release than is AIII. Depletion of renal norepinephrine by reserpine (10 mg/kg, i.p.) or pretreatment of slices with papaverine (1 X 10(-4) M) did not block the action of AII. The data give evidence for a direct action of AII on the juxtaglomerular cells independent of an interaction with either the sympathetic nervous system or the arteriolar baroreceptor and suggest that the intrarenal receptors that mediate AII-induced inhibition of renin release differ from AII receptors in the adrenal cortex.

scholarly journals The Amino-Terminal Region of Major Capsid Protein P3 Is Essential for Self-Assembly of Single-Shelled Core-Like Particles of Rice Dwarf Virus

2004 ◽  
Vol 78 (6) ◽  
pp. 3145-3148 ◽  
Author(s):  
Kyoji Hagiwara ◽  
Takahiko Higashi ◽  
Naoyuki Miyazaki ◽  
Hisashi Naitow ◽  
R. Holland Cheng ◽  
...  
Keyword(s):  
Self Assembly ◽  
Major Capsid Protein ◽  
Core Protein ◽  
Terminal Region ◽  
Dwarf Virus ◽  
Rice Dwarf Virus ◽  
Amino Terminal ◽  
The Core ◽  
Baculovirus System ◽  
Terminal Amino

ABSTRACT The core protein P3 of Rice dwarf virus constructs asymmetric dimers, one of which is inserted by the amino-terminal region of another P3 protein. The P3 proteins with serial amino-terminal deletions, expressed in a baculovirus system, formed particles with gradually decreasing stability. The capacity for self-assembly disappeared when 52 of the amino-terminal amino acids had been deleted. These results demonstrated that insertion of the amino-terminal arm of one P3 protein into another appears to play an important role in stabilizing the core particles.

Soil nitrogen and lodgepole pine seedling responses to five years of legume cover

1998 ◽  
Vol 74 (4) ◽  
pp. 578-582 ◽  
Author(s):  
J. M. Kranabetter ◽  
R. Trowbridge
Keyword(s):  
Soil Nitrogen ◽  
Forest Floor ◽  
Pinus Contorta ◽  
Lodgepole Pine ◽  
Seeding Density ◽  
Total N ◽  
Pine Seedlings ◽  
Key Words Nitrogen Fixation ◽  
Multiple Species ◽  
Key Words Nitrogen

Legumes were tested for their ability to increase soil N content and improve growth of lodgepole pine (Pinus contorta Dougl. ex Loud.) seedlings in west-central British Columbia. A trial with alsike clover at varying densities were tested at one site, while three legume species (alsike clover, birdsfoot trefoil, and white clover) were tested on a second site. After five years of legume cover, mineralizable N mass of the forest floor were 0.5 to 4.5 times those of controls. Total N of the forest floor more than doubled in the seeding density study compared with controls, but was insignificant in the multiple species study. Despite observed increases in soil nitrogen, lodgepole pine growth was not enhanced by the legume treatments. Factors such as N immobilization, root distribution, low S levels, and competition for B may have limited the response of lodgepole pine seedlings to additions of biologically fixed-N. Key words: nitrogen-fixation, legumes, lodgepole pine, soil nitrogen

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