Functional Replacement of Hamster Lysyl-tRNA Synthetase by the Yeast Enzyme Requires Cognate Amino Acid Sequences for Proper tRNA Recognition†

Biochemistry ◽  
1996 ◽  
Vol 35 (48) ◽  
pp. 15322-15331 ◽  
Author(s):  
Fabrice Agou ◽  
Sophie Quevillon ◽  
Pierre Kerjan ◽  
Marie-Thérèse Latreille ◽  
Marc Mirande
Keyword(s):  
Amino Acid ◽  
Trna Synthetase ◽  
Amino Acid Sequences ◽  
Trna Recognition ◽  
Functional Replacement

Identification of an amino acid region supporting specific methionyl-tRNA synthetase: tRNA recognition

1989 ◽  
Vol 208 (3) ◽  
pp. 429-443 ◽  
Author(s):  
Patrice Mellot ◽  
Yves Mechulam ◽  
Daniel Le Corre ◽  
Sylvain Blanquet ◽  
Guy Fayat
Keyword(s):  
Amino Acid ◽  
Trna Synthetase ◽  
Trna Recognition ◽  
Amino Acid Region ◽  
Methionyl Trna Synthetase ◽  
Acid Region

scholarly journals Surfeit locus gene homologs are widely distributed in invertebrate genomes.

1996 ◽  
Vol 16 (10) ◽  
pp. 5591-5596 ◽  
Author(s):  
N Armes ◽  
M Fried
Keyword(s):  
Endoplasmic Reticulum ◽  
Drosophila Melanogaster ◽  
Amino Acid ◽  
Integral Membrane Protein ◽  
Trna Synthetase ◽  
Amino Acid Sequences ◽  
Gene Clustering ◽  
Regulatory Requirement ◽  
C Elegans ◽  
Mouse Protein

The mouse Surfeit locus contains six sequence-unrelated genes (Surf-1 to -6) arranged in the tightest gene cluster so far described for mammals. The organization and juxtaposition of five of the Surfeit genes (Surf-1 to -5) are conserved between mammals and birds, and this may reflect a functional or regulatory requirement for the gene clustering. We have undertaken an evolutionary study to determine whether the Surfeit genes are conserved and clustered in invertebrate genomes. Drosophila melanogaster and Caenorhabditis elegans homologs of the mouse Surf-4 gene, which encodes an integral membrane protein associated with the endoplasmic reticulum, have been isolated. The amino acid sequences of the Drosophila and C. elegans homologs are highly conserved in comparison with the mouse Surf-4 protein. In particular, a dilysine motif implicated in endoplasmic reticulum localization of the mouse protein is conserved in the invertebrate homologs. We show that the Drosophila Surf-4 gene, which is transcribed from a TATA-less promoter, is not closely associated with other Drosophila Surfeit gene homologs but rather is located upstream from sequences encoding a homolog of a yeast seryl-tRNA synthetase protein. There are at least two closely linked Surf-3/rpL7a genes or highly polymorphic alleles of a single Surf-3/rpL7a gene in the C. elegans genome. The chromosomal locations of the C. elegans Surf-1, Surf-3/rpL7a, and Surf-4 genes have been determined. In D. melanogaster the Surf-3/rpL7a, Surf-4, and Surf-5 gene homologs and in C. elegans the Surf-1, Surf-3/rpL7a, Surf-4, and Surf-5 gene homologs are located on completely different chromosomes, suggesting that any requirement for the tight clustering of the genes in the Surfeit locus is restricted to vertebrate lineages.

Cloning and Sequencing of the Histidine Decarboxylase Gene from Photobacterium phosphoreum and its Functional Expression in Escherichia coli

2006 ◽  
Vol 69 (8) ◽  
pp. 1768-1776 ◽  
Author(s):  
HIDEAKI MORII ◽  
KENTARO KASAMA ◽  
RAUL HERRERA-ESPINOZA
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Histidine Decarboxylase ◽  
Halophilic Bacteria ◽  
Trna Synthetase ◽  
Amino Acid Sequences ◽  
Photobacterium Phosphoreum ◽  
Bootstrap Support ◽  
Amino Acid Permease ◽  
E Coli

The major causative agent of scombroid poisoning is histamine formed by bacterial decarboxylation of histidine. We reported previously that histamine was exclusively formed by the psychrotrophic halophilic bacteria Photobacterium phosphoreum in scombroid fish during storage at or below 10°C. Moreover, histamine-forming ability was affected by two histidine decarboxylases (HDCs): constitutive and inducible enzymes. In this study, the gene encoding P. phosphoreum HDC was cloned into Escherichia coli and sequenced. A sequence analysis of the DNA corresponding to the hdc gene revealed an open reading frame of 1,140 bp coding for a pyridoxal-5′-phosphate-dependent HDC of 380 amino acid residues with a predicted molecular mass of 42.6 kDa. The HDC amino acid sequences formed a phylogenetic clade with strong bootstrap support and revealed high sequence similarities among the P. phosphoreum isolate and species of the family Enterobacteriaceae and a separate phylogenetic branch with the lowest sequence similarity between the isolate and the taxonomically closer Listonella anguillarum. The T7 promoter was used to overexpress the hdc gene in E. coli cells. The recombinant clone, E. coli BL21(DE3), displayed significant levels of HDC activity. The recombinant hdc gene was suggested to code the inducible HDC; therefore, the optimum reaction conditions of the recombinant HDC were similar to those of the inducible HDC in the P. phosphoreum isolate. In addition, a putative catabolite-repressor protein binding site, amino acid permease gene, and histidine-tRNA synthetase gene were found in flanking regions of the hdc gene.

scholarly journals In-silico analysis of Salmonella typhimurium and E.coli Methionyl tRNA synthetase at primary, secondary, tertiary level with protein disorder and functional association of differences

2016 ◽  
Author(s):  
Prabhakar B. Ghorpade ◽  
Pooja Kadu ◽  
Amit Pandey ◽  
Yogesh Banger ◽  
Bhaskar Sharma
Keyword(s):  
Amino Acid ◽  
Salmonella Typhimurium ◽  
Tertiary Structure ◽  
3D Structure ◽  
In Silico Analysis ◽  
Trna Synthetase ◽  
Amino Acid Sequences ◽  
Functional Protein ◽  
Functional Differences ◽  
Methionyl Trna Synthetase

AbstractThe identification changes in amino acid for same protein in closely related species are necessary in order to identify its effect at various structural and functional levels. Salmonella typhimurium and E.coli Methionyl tRNA synthetase taken in current study as these bacteria are closely related to each other and have fewer differences in amino acid sequences for MetG. This study helps to identify various structural and functional differences at primary, secondary and tertiary levels, with functional differences by Docking study with Methionine. Study involves analysis of differences based on observation of differences in modeled 3D protein for sequences available at NCBI and its comparison with Known 3D structure. As sequences difference are in functional protein from non-mutant species, the differences are analysed in context of Primary, secondary, tertiary structure differences, Disorder differences, and docking differences.

Diversity of Primary Structures of the Carboxy-terminal Regions of Mammalian Fibrinogen Aα-Chains

1993 ◽  
Vol 69 (04) ◽  
pp. 351-360 ◽  
Author(s):  
Masahiro Murakawa ◽  
Takashi Okamura ◽  
Takumi Kamura ◽  
Tsunefumi Shibuya ◽  
Mine Harada ◽  
...  
Keyword(s):  
Amino Acid ◽  
Rhesus Monkey ◽  
Syrian Hamster ◽  
Tandem Repeats ◽  
Mammalian Species ◽  
Amino Acid Sequences ◽  
Point Of View ◽  
Cross Linking ◽  
Amino Terminal ◽  
Rgd Sequence

SummaryThe partial amino acid sequences of fibrinogen Aα-chains from five mammalian species have been inferred by means of the polymerase chain reaction (PCR). From the genomic DNA of the rhesus monkey, pig, dog, mouse and Syrian hamster, the DNA fragments coding for α-C domains in the Aα-chains were amplified and sequenced. In all species examined, four cysteine residues were always conserved at the homologous positions. The carboxy- and amino-terminal portions of the α-C domains showed a considerable homology among the species. However, the sizes of the middle portions, which corresponded to the internal repeat structures, showed an apparent variability because of several insertions and/or deletions. In the rhesus monkey, pig, mouse and Syrian hamster, 13 amino acid tandem repeats fundamentally similar to those in humans and the rat were identified. In the dog, however, tandem repeats were found to consist of 18 amino acids, suggesting an independent multiplication of the canine repeats. The sites of the α-chain cross-linking acceptor and α2-plasmin inhibitor cross-linking donor were not always evolutionally conserved. The arginyl-glycyl-aspartic acid (RGD) sequence was not found in the amplified region of either the rhesus monkey or the pig. In the canine α-C domain, two RGD sequences were identified at the homologous positions to both rat and human RGD S. In the Syrian hamster, a single RGD sequence was found at the same position to that of the rat. Triplication of the RGD sequences was seen in the murine fibrinogen α-C domain around the homologous site to the rat RGDS sequence. These findings are of some interest from the point of view of structure-function and evolutionary relationships in the mammalian fibrinogen Aα-chains.

Bovine Factors X1And X2: Activation Peptide Based Chromatographic Differences

1979 ◽  
Author(s):  
Takashi Morita ◽  
Craig Jackson
Keyword(s):  
Amino Acid ◽  
Anion Exchange ◽  
Gel Filtration ◽  
Heart Association ◽  
Personal Communication ◽  
Exchange Chromatography ◽  
Amino Acid Sequences ◽  
Factor X ◽  
Activation Peptide ◽  
Activation Peptides

Bovine Factor X is eluted in two forms (X1and X2) from anion exchange chromatographic columns. These two forms have indistinguishable amino acid compositions, molecular weights and specific activities. The amino acid sequences containing the γ-carboxyglutamic acid residues have been shown to be identical in X1 and X2(H. Morris, personal communication). An activation peptide is released from the N-terminal region of the heavy chain of Factor X by an activator from Russell’s viper venom. This peptide can be isolated after activation by gel filtration on Sephadex G-100 under nondenaturing conditions. The activation peptides from a mixture of Factors X1 and X2 were separated into two forms by anion-exchange chromatography. The activation peptide (AP1) which eluted first was shown to be derived from Factor X1. while the activation peptiae (AP2) which eluted second was shown to be derived from X2 on the basis of chromatographic separations carried out on Factors X1 and X2 separately. Factor Xa was eluted as a symmetrical single peak. On the basis of these and other data characterizing these products, we conclude that the difference between X1 and X2 are properties of the structures of the activation peptides. (Supported by a grant HL 12820 from the National Heart, Lung and Blood Institute. C.M.J. is an Established Investigator of the American Heart Association).

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