scholarly journals A Second and Unusual pucBA Operon of Rhodobacter sphaeroides 2.4.1: Genetics and Function of the Encoded Polypeptides

2003 ◽  
Vol 185 (20) ◽  
pp. 6171-6184 ◽  
Author(s):  
Xiaohua Zeng ◽  
Madhu Choudhary ◽  
Samuel Kaplan
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Complex Formation ◽  
Rhodobacter Sphaeroides ◽  
Sequence Data ◽  
Sole Source ◽  
Amino Acid Derivative ◽  
Dna Sequence Data ◽  
And Function ◽  
High Degree

ABSTRACT A new operon (designated the puc2BA operon) displaying a high degree of similarity to the original pucBA genes of Rhodobacter sphaeroides 2.4.1 (designated puc1) was identified and studied genetically and biochemically. The puc2B-encoded polypeptide is predicted to exhibit 94% identity with the original β-apoprotein. The puc2A-encoded polypeptide is predicted to be much larger (263 amino acids) than the 54-amino-acid puc1A-encoded polypeptide. In the first 48 amino acids of the puc2A-encoded polypeptide there is 58% amino acid sequence identity to the original puc1A-encoded polypeptide. We found that puc2BA is expressed, and DNA sequence data suggested that puc2BA is regulated by the PpsR/AppA repressor-antirepressor and FnrL. Employing genetic and biochemical approaches, we obtained evidence that the puc2B-encoded polypeptide is able to enter into LH2 complex formation, but neither the full-length puc2A-encoded polypeptide nor its N-terminal 48-amino-acid derivative is able to enter into LH2 complex formation. Thus, the sole source of α-polypeptides for the LH2 complex is puc1A. The role of the puc1C-encoded polypeptide was also determined. We found that the presence of this polypeptide is essential for normal levels of transcription and translation of the puc1 operon but not for transcription and translation of the puc2 operon. Thus, the puc1C gene product appears to have both transcriptional and posttranscriptional roles in LH2 formation. Finally, the absence of any LH2 complex when puc1B was deleted in frame was surprising since we know that in the presence of functional puc2BA, approximately 30% of the LH2 complexes normally observed contain a puc2B-encoded β-polypeptide.

scholarly journals Amino Acids and the Early Mammalian Embryo: Origin, Fate, Function and Life-Long Legacy

2021 ◽  
Vol 18 (18) ◽  
pp. 9874
Author(s):  
Henry J. Leese ◽  
Paul McKeegan ◽  
Roger G Sturmey
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Culture Media ◽  
Early Embryo ◽  
Amino Acid Derivative ◽  
Cellular Functions ◽  
Traditional Role ◽  
Mammalian Embryo ◽  
Early Mammalian Embryo ◽  
And Function

Amino acids are now recognised as having multiple cellular functions in addition to their traditional role as constituents of proteins. This is well-illustrated in the early mammalian embryo where amino acids are now known to be involved in intermediary metabolism, as energy substrates, in signal transduction, osmoregulation and as intermediaries in numerous pathways which involve nitrogen metabolism, e.g., the biosynthesis of purines, pyrimidines, creatine and glutathione. The amino acid derivative S-adenosylmethionine has emerged as a universal methylating agent with a fundamental role in epigenetic regulation. Amino acids are now added routinely to preimplantation embryo culture media. This review examines the routes by which amino acids are supplied to the early embryo, focusing on the role of the oviduct epithelium, followed by an outline of their general fate and function within the embryo. Functions specific to individual amino acids are then considered. The importance of amino acids during the preimplantation period for maternal health and that of the conceptus long term, which has come from the developmental origins of health and disease concept of David Barker, is discussed and the review concludes by considering the potential utility of amino acid profiles as diagnostic of embryo health.

PSVI-13 Amino Acid Supplementation During the Adaptation Period Did Not Affect the Standardized Ileal Digestibility of Amino Acids in Corn and Soybean Meal Fed to Pigs

2021 ◽  
Vol 99 (Supplement_1) ◽  
pp. 200-201
Author(s):  
Hyunjun Choi ◽  
Sun Jong You ◽  
Beob Gyun G Kim
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Soybean Meal ◽  
Latin Square ◽  
Sole Source ◽  
Adaptation Period ◽  
Amino Acid Supplementation ◽  
Ileal Digestibility ◽  
Indispensable Amino Acids ◽  
Dietary Treatments

Abstract The objective was to determine the influence of amino acid (AA) supplementation during the adaptation period on the ileal digestibility of crude protein and AA in corn and soybean meal (SBM). Six barrows with an initial body weight of 30.9 ± 2.6 kg fitted with a T-cannula in the distal ileum were assigned to a 6 × 6 Latin square design with 6 dietary treatments and 6 periods. Two experimental diets contained corn or SBM as the sole source of AA and an N-free diet was additionally prepared. For AA supplementation groups, an AA mixture consisted of Gly, Lys, Met, Thr, Trp, Ile, Val, His, and Phe was added to the corn diet and the N-free diet at the expense of cornstarch, and an AA mixture of Lys, Met, and Thr was added to the SBM diet. All diets contained 0.5% of chromic oxide. The 6 experimental diets were fed to the pigs for 4 and half days, and the 3 diets containing AA mixture were switched to the respective diets without AA mixture during the following 2 and half days. Ileal digesta were collected during the last 2 days. The addition of AA mixture during the adaptation period caused increased apparent ileal digestibility of Arg and Trp in corn (P < 0.05), but did not affect that in SBM. The addition of AA mixture during the adaptation period caused increased apparent ileal digestibility of Pro and Gly regardless of feed ingredient (P < 0.05), but did not affect that of other AA. All AA except Pro in corn and SBM were unaffected by the addition of AA mixture during the adaptation period. In conclusion, the addition of amino acid during the adaptation period does not affect the standardized ileal digestibility of indispensable amino acids in feed ingredients.

scholarly journals Amino Acid-Mediated Induction of the Basic Amino Acid-Specific Outer Membrane Porin OprD from Pseudomonas aeruginosa

1999 ◽  
Vol 181 (17) ◽  
pp. 5426-5432 ◽  
Author(s):  
Martina M. Ochs ◽  
Chung-Dar Lu ◽  
Robert E. W. Hancock ◽  
Ahmed T. Abdelal
Keyword(s):  
Amino Acids ◽  
Pseudomonas Aeruginosa ◽  
Amino Acid ◽  
Regulatory Protein ◽  
Basic Amino Acid ◽  
Sole Source ◽  
Activation Mechanism ◽  
Beta Lactam ◽  
Mobility Shift ◽  
Carbon And Nitrogen

ABSTRACT Pseudomonas aeruginosa can utilize arginine and other amino acids as both carbon and nitrogen sources. Earlier studies have shown that the specific porin OprD facilitates the diffusion of basic amino acids as well as the structurally analogous beta-lactam antibiotic imipenem. The studies reported here showed that the expression of OprD was strongly induced when arginine, histidine, glutamate, or alanine served as the sole source of carbon. The addition of succinate exerted a negative effect on induction ofoprD, likely due to catabolite repression. The arginine-mediated induction was dependent on the regulatory protein ArgR, and binding of purified ArgR to its operator upstream of theoprD gene was demonstrated by gel mobility shift and DNase assays. The expression of OprD induced by glutamate as the carbon source, however, was independent of ArgR, indicating the presence of more than a single activation mechanism. In addition, it was observed that the levels of OprD responded strongly to glutamate and alanine as the sole sources of nitrogen. Thus, that the expression ofoprD is linked to both carbon and nitrogen metabolism ofPseudomonas aeruginosa.

scholarly journals Amino acid sequence of the encephalitogenic basic protein from human myelin

1971 ◽  
Vol 123 (1) ◽  
pp. 57-67 ◽  
Author(s):  
P. R. Carnegie
Keyword(s):  
Amino Acids ◽  
Central Nervous System ◽  
Nervous System ◽  
Amino Acid ◽  
Basic Protein ◽  
Structure And Function ◽  
Autoimmune Encephalomyelitis ◽  
The Central Nervous System ◽  
And Function ◽  
Experimental Autoimmune

Myelin from the central nervous system contains an unusual basic protein, which can induce experimental autoimmune encephalomyelitis. The basic protein from human brain was digested with trypsin and other enzymes and the sequence of the 170 amino acids was determined. The localization of the encephalitogenic determinants was described. Possible roles for the protein in the structure and function of myelin are discussed.

Sorption of α-amino-acids by copper montmorillonite

Clay Minerals ◽  
1967 ◽  
Vol 7 (2) ◽  
pp. 167-176 ◽  
Author(s):  
W. Bodenheimer ◽  
L. Heller
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Complex Formation ◽  
Glutamic Acid ◽  
Acid Complex ◽  
X Ray ◽  
Ray Methods

AbstractSorption of an acidic, amphoteric, sulphur containing and basic α-amino-acid (glutamic acid, glycine, methionine and lysine) by copper montmorillonite was studied by chemical and X-ray methods. With glutamic acid complex formation occurs only in solution but increasing basicity of the aminoacid favours complex formation in the clay interlayers.

Source and function of urinary ammonia in the alligator

1959 ◽  
Vol 197 (4) ◽  
pp. 873-879 ◽  
Author(s):  
Roland A. Coulson ◽  
Thomas Hernandez
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Acid Level ◽  
Amino Acid Level ◽  
Plasma Amino Acid ◽  
Plasma Amino Acids ◽  
Renal Reabsorption ◽  
And Function ◽  
Phosphate Solutions

The rate of renal deamination of 18 amino acids was determined by injecting them into alligators and measuring the ammonia excreted. Not only did glycine, alanine, glutamine and leucine account for nearly half of the plasma amino acids, they were also deaminated more rapidly than any of the others. In view of this it was concluded that these four amino acids are the natural precursors of urinary NH3 in the alligator. Increased NH3 and CO2 excretion following glycine injections resulted in increased renal reabsorption of Na and Cl when NaCl was injected and increased Na reabsorption when NaHCO3 or Na phosphate solutions were injected. The fact that excess NH4HCO3 excretion enhances salt reabsorption independent of plasma pH makes it probable that the excretion of N is the chief function of the ammonia mechanism and that salt conservation is incidental. Insulin decreased the plasma amino acid level and drastically reduced the NH3 excretion. With the decrease in ammonia, NaCl and NaHCO3 were excreted in increased amounts.

scholarly journals Excessive heating of 00-rapeseed meal reduces not only amino acid digestibility but also metabolizable energy when fed to growing pigs

2020 ◽  
Vol 98 (7) ◽  
Author(s):  
Maryane S F Oliveira ◽  
Markus K Wiltafsky-Martin ◽  
Hans H Stein
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Basal Diet ◽  
Rapeseed Meal ◽  
Sole Source ◽  
Heating Time ◽  
Growing Pigs ◽  
Metabolizable Energy ◽  
Negative Effects ◽  
Ileal Digestibility

Abstract Two experiments were conducted to test the hypothesis that both the degree of heating and the time that heat is applied will affect the concentration of DE and ME, and the apparent ileal digestibility (AID) and the standardized ileal digestibility (SID) of amino acids (AA) in 00-rapeseed meal (00-RSM) fed to growing pigs. The nine treatments were prepared using a conventional 00-RSM that was either not autoclaved or autoclaved at 110 °C for 15 or 30 min or at 150 °C for 3, 6, 9, 12, 15, or 18 min. In experiment 1, 20 growing barrows with an average initial BW of 21.2 ± 1.2 kg were randomly allotted to the 10 diets in a replicated 10 × 4 Youden square with 10 diets and four periods in each square. A corn-based basal diet and nine diets containing corn and each source of 00-RSM were formulated. Urine and fecal samples were collected for 5 d after 7 d of adaptation. In experiment 2, nine diets contained one of the nine sources of 00-RSM as the sole source of AA, and an N-free diet that was used to measure basal endogenous losses of AA and CP was formulated. Twenty growing barrows with an initial BW of 69.8 ± 5.7 kg had a T-cannula installed in the distal ileum and were allotted to a 10 × 7 Youden square design with 10 diets and 7 periods. Ileal digesta were collected on days 6 and 7 of each 7-d period. Results from the experiments indicated that there were no effects of autoclaving at 110 °C on DE and ME or on AID and SID of AA in 00-RSM, but DE and ME, and AID and SID of AA were less (P < 0.01) if 00-RSM was autoclaved at 150 °C compared with 110 °C. At 150 °C, there were decreases (quadratic, P < 0.05) in DE and ME, and in AID and SID of AA as heating time increased. In conclusion, autoclaving at 110 °C did not affect ME or SID of AA in 00-RSM, but autoclaving at 150 °C had negative effects on ME and SID of AA and the negative effects increased as heating time increased.

Improved function with amino acids in the isolated perfused kidney

1982 ◽  
Vol 243 (3) ◽  
pp. F284-F292 ◽  
Author(s):  
F. H. Epstein ◽  
J. T. Brosnan ◽  
J. D. Tange ◽  
B. D. Ross
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Glutathione Depletion ◽  
Sodium Reabsorption ◽  
Thick Ascending Limb ◽  
Amino Acid Supplementation ◽  
Renal Structure ◽  
Improved Function ◽  
And Function ◽  
Renal Concentrating Capacity

When isolated rat kidneys are perfused with glucose as the only substrate, there is a progressive diminution in glomerular filtration rate and fractional reabsorption of sodium. This is most marked after 1 h. Renal glutathione content rapidly falls and is less than 30% of control levels after 1 h. Renal concentrating ability is markedly impaired and structural lesions are consistently observed in cells lining the thick ascending limb of Henle's loop. Addition of 20 physiologic amino acids including cysteine to the perfusate prevents the fall in renal glutathione, prevents the anatomical damage to ascending limb cells, permits GFR and fractional sodium reabsorption to remain high and close to their initial levels for as long as 4 h, and improves renal concentrating capacity. If amino acid supplementation is limited to three precursors of glutathione--cysteine, glycine, and glutamic acid--renal glutathione content is preserved and concentrating ability is improved, but GFR and fractional sodium reabsorption are not maintained as well as with comprehensive amino acid supplements. The results suggest that amino acid deficiency and glutathione depletion may contribute to disturbances in renal structure and function.

scholarly journals Partial amino acid sequence and mRNA analysis of cytosolic pyridoxine-beta-d-glucoside hydrolase from porcine intestinal mucosa: proposed derivation from the lactase-phlorizin hydrolase gene

2004 ◽  
Vol 380 (1) ◽  
pp. 211-218 ◽  
Author(s):  
Chi-Wah TSEUNG ◽  
Laura G. McMAHON ◽  
Jorge VÁZQUEZ ◽  
Jan POHL ◽  
Jesse F. GREGORY
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Northern Blot ◽  
Sequence Data ◽  
Cdna Probe ◽  
Protein Mass ◽  
Sds Page ◽  
Mrna Analysis ◽  
Hydrolysis Of

We have previously identified and purified a novel β-glucosidase, designated PNGH (pyridoxine-5´-β-d-glucoside hydrolase), from the cytosolic fraction of pig intestinal mucosal. PNGH catalyses the hydrolysis of PNG (pyridoxine-5´-β-d-glucoside), a plant derivative of vitamin B6 that exhibits partial nutritional bioavailability in humans and animals. Preliminary amino acid sequence analysis indicated regions of close similarity of PNGH to the precursor form of LPH (lactase–phlorizin hydrolase), the β-glucosidase localized to the brush-border membrane. We report in the present study amino acid sequence data for PNGH and results of Northern blot analyses, upon which we propose a common genomic origin of PNGH and LPH. Internal Edman sequencing of the PNGH band isolated by SDS/PAGE yielded data for 16 peptides, averaging 10.8 amino acids in length. These peptides from PNGH (approx. 140 kDa) were highly similar to sequences existing over most of the length of the >200 kDa precursor of rabbit LPH; however, we found no PNGH sequences that corresponded to approx. 350 amino acids between positions 463 and 812 of the LPH precursor, a region encoded by exon 7 of the LPH precursor gene (amino acids 568–784), and no sequences that corresponded to regions near the N-terminus. MS analysis of tryptic peptides yielded 25 peptides, averaging 15 amino acids, with masses that matched segments of the rabbit LPH precursor. Northern blot analysis of pig and human small intestinal polyadenylated mRNA using a non-specific LPH cDNA probe showed an expected approx. 6 kb transcript of the LPH precursor, but also an approx. 4 kb transcript that was consistent with the size predicted from the PNGH protein mass. Using a probe specific to the region encoded by exon 7, hybridization occurred only with the 6 kb transcript. Based on these observations, we propose that both PNGH and LPH enzymes have the same genomic origin, but differ in transcriptional and, possibly, post-translational processing.

scholarly journals Can Power Laws Help Us Understand Gene and Proteome Information?

2013 ◽  
Vol 2013 ◽  
pp. 1-10 ◽  
Author(s):  
J. A. Tenreiro Machado ◽  
António C. Costa ◽  
Maria Dulce Quelhas
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Genetic Code ◽  
Protein Function ◽  
Sequence Data ◽  
Proteome Analysis ◽  
Power Laws ◽  
Linear Sequence ◽  
Graphical Visualization

Proteins are biochemical entities consisting of one or more blocks typically folded in a 3D pattern. Each block (a polypeptide) is a single linear sequence of amino acids that are biochemically bonded together. The amino acid sequence in a protein is defined by the sequence of a gene or several genes encoded in the DNA-based genetic code. This genetic code typically uses twenty amino acids, but in certain organisms the genetic code can also include two other amino acids. After linking the amino acids during protein synthesis, each amino acid becomes a residue in a protein, which is then chemically modified, ultimately changing and defining the protein function. In this study, the authors analyze the amino acid sequence using alignment-free methods, aiming to identify structural patterns in sets of proteins and in the proteome, without any other previous assumptions. The paper starts by analyzing amino acid sequence data by means of histograms using fixed length amino acid words (tuples). After creating the initial relative frequency histograms, they are transformed and processed in order to generate quantitative results for information extraction and graphical visualization. Selected samples from two reference datasets are used, and results reveal that the proposed method is able to generate relevant outputs in accordance with current scientific knowledge in domains like protein sequence/proteome analysis.

Sign in / Sign up

Export Citation Format

Share Document