scholarly journals Molecular cloning of chicken aggrecan. Structural analyses

1992 ◽  
Vol 288 (3) ◽  
pp. 903-910 ◽  
Author(s):  
L Chandrasekaran ◽  
M L Tanzer
Keyword(s):  
Amino Acids ◽  
Molecular Cloning ◽  
Chondroitin Sulphate ◽  
Repetitive Sequences ◽  
Amino Acid Sequences ◽  
The Other ◽  
Generic Model ◽  
Coding Region ◽  
Linear Arrangement ◽  
Keratan Sulphate

The large, aggregating chondroitin sulphate proteoglycan of cartilage, aggrecan, has served as a generic model of proteoglycan structure. Molecular cloning of aggrecans has further defined their amino acid sequences and domain structures. In this study, we have obtained the complete coding sequence of chicken sternal cartilage aggrecan by a combination of cDNA and genomic DNA sequencing. The composite sequence is 6117 bp in length, encoding 1951 amino acids. Comparison of chicken aggrecan protein primary structure with rat, human and bovine aggrecans has disclosed both similarities and differences. The domains which are most highly conserved at 70-80% identity are the N-terminal domains G1 and G2 and the C-terminal domain G3. The chondroitin sulphate domain of chicken aggrecan is smaller than that of rat and human aggrecans and has very distinctive repeat sequences. It has two separate sections, one comprising 12 consecutive Ser-Gly-Glu repeats of 20 amino acids each, adjacent to the other which has 23 discontinuous Ser-Gly-Glu repeats of 10 amino acids each; this latter region, N-terminal to the former one, appears to be unique to chicken aggrecan. The two regions contain a total of 94 potential chondroitin sulphate attachment sites. Genomic comparison shows that, although chicken exons 11-14 are identical in size to the rat and human exons, chicken exon 10 is the smallest of the three species. This is also reflected in the size of its chondroitin sulphate coding region and in the total number of Ser-Gly pairs. The putative keratan sulphate domain shows 31-45% identity with the other species and lacks the repetitive sequences seen in the others. In summary, while the linear arrangement of specific domains of chicken aggrecan is identical to that in the aggrecans of other species, and while there is considerable identity of three separate domains, chicken aggrecan demonstrates unique features, notably in its chondroitin sulphate domain and its keratan sulphate domain. Thus different variants of chondroitin sulphate and keratan sulphate domains may have evolved separately to fulfil specific biochemical and physiological functions.

scholarly journals Nucleotide and derived amino acid sequences of a cDNA coding for pre-uteroglobin from the lung of the hare (Lepus capensis)

1986 ◽  
Vol 235 (3) ◽  
pp. 895-898 ◽  
Author(s):  
M S López de Haro ◽  
A Nieto
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence ◽  
Amino Acid Sequences ◽  
Untranslated Regions ◽  
Coding Region ◽  
Homologous Proteins ◽  
Lepus Capensis ◽  
Rabbit Gene

An almost full-length cDNA coding for pre-uteroglobin from hare lung was cloned and sequenced. The derived amino acid sequence indicated that hare pre-uteroglobin contained 91 amino acids, including a signal peptide of 21 residues. Comparison of the nucleotide sequence of hare pre-uteroglobin cDNA with that previously reported for the rabbit gene indicated five silent point substitutions and six others leading to amino acid changes in the coding region. The untranslated regions of both pre-uteroglobin mRNAs were very similar. The amino acid changes observed are discussed in relation to the different progesterone-binding abilities of both homologous proteins.

scholarly journals Amino acid sequences around the cystine residues in horse growth hormone

1968 ◽  
Vol 109 (1) ◽  
pp. 19-24 ◽  
Author(s):  
Louise Oliver ◽  
Anne Stockell Hartree
Keyword(s):  
Amino Acids ◽  
Growth Hormone ◽  
Amino Acid ◽  
Growth Hormones ◽  
Amino Acid Sequences ◽  
The Other ◽  
Published Data ◽  
C Terminus

The cystine-containing peptides of horse growth hormone were isolated and their amino acid sequences determined. Four unique half-cystine residues occur in two peptides, one containing 11 and the other, at the C-terminus of the protein, 15 amino acids. These sequences are compared with published data on growth hormones from other species.

Characterization of the mouse thyrotrophin-releasing hormone receptor gene: an exon corresponds to a deletion in the rat cDNA

1993 ◽  
Vol 11 (2) ◽  
pp. 141-149 ◽  
Author(s):  
S M Duthie ◽  
P L Taylor ◽  
K A Eidne
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Stop Codon ◽  
Amino Acid Sequences ◽  
R Gene ◽  
Coding Region ◽  
Thyrotrophin Releasing Hormone ◽  
Exon 2 ◽  
Exon 4

ABSTRACT The cloning and characterization of the mouse TRH receptor (TRH-R) gene revealed an untranslated exon (exon 1), a single intron and an upstream dinucleotide repeat sequence (d(TG)16.d(AG)21) in the 5′ untranslated region (UTR). The coding region was contained almost entirely on a second exon (exon 2), with the final amino acid and stop codon at the COOH terminus of the gene encoded by a third exon (exon 3) flanked by two introns. The 3′ UTR was contained on the remainder of exon 3 and on the final exon (exon 4). Exon 3 (228 bp) corresponds exactly to a 228 bp deletion that exists in the rat TRH-R cDNA, but not in the mouse cDNA. The mouse TRH-R cDNA encodes a protein of 393 amino acids which is 96% homologous to the rat TRH-R protein of 412 amino acids, but is 19 amino acids shorter at its COOH terminus. The coding sequence for these 19 amino acids (plus 1 extra amino acid) does exist in the mouse TRH-R gene, but the sequence is encoded by exon 4, separated from the rest of the coding region by the stop codon and 223 bp of 3′ UTR on exon 3. Splicing of exon 3 in the mouse TRH-R gene would remove the last amino acid, the stop codon and the 223 bp of 3′ UTR, allowing transcription to continue into the 3′ UTR on exon 4, which encodes the 19 extra amino acids found in the rat cDNA. This would then result in an alternative 412 amino acid version of the mouse TRH-R protein, with 95% homology to the rat TRH-R. This study focused on the structural differences in the intracellular COOH-terminal tail of the receptor, which is known to be a functionally important domain in other members of the G protein-coupled receptor family. We have also recently characterized the human TRH-R cDNA, which revealed a third variant at the COOH terminus. Comparisons between mouse, rat and human TRH-Rs show that the amino acid sequences are virtually identical. However, significant differences between these species exist at the COOH terminus, with each TRH-R having a unique form of the COOH-terminal tail, beginning at exactly the same site and encoding 1, 20 and 6 amino acids in the mouse, rat and human respectively.

Die primäre Proteinstruktur von Stämmen des Tabakmosaikvirus

1969 ◽  
Vol 24 (7) ◽  
pp. 870-877 ◽  
Author(s):  
J. Jauregui-Adell ◽  
I. Hindennach ◽  
H. G. Wittmann
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Coat Protein ◽  
Tobacco Mosaic Virus ◽  
Primary Structure ◽  
Amino Acid Sequences ◽  
The Other ◽  
Protein Subunit ◽  
Tryptic Peptides ◽  
Tmv Strains

The sequence of amino acids within the coat protein of the strain Holmes rib grass of tobacco mosaic virus (TMV) has been determined. In this communication the amino acid compositions of the coat protein and of all tryptic peptides are reported. Furthermore the experimental details are given for the elucidation of the amino acid sequences within the first three tryptic peptides, containing 61 amino acids.It has been found that the strain Holmes rib grass differs very extensively in the primary structure from the other TMV strains whose sequences are known. It differs from each of the other strains in more than 50% of the amino acid positions and it contains two amino acids less per protein subunit than the other TMV strains.

Die primäre Proteinstruktur von Stämmen des Tabakmosaikvirus

1969 ◽  
Vol 24 (7) ◽  
pp. 877-885 ◽  
Author(s):  
H. G. Wittmann ◽  
I. Hindennach ◽  
B. Wittmann-Liebold
Keyword(s):  
Experimental Data ◽  
Amino Acids ◽  
Amino Acid ◽  
Coat Protein ◽  
Amino Acid Sequence ◽  
Spatial Structure ◽  
Amino Acid Sequences ◽  
The Other ◽  
Tryptic Peptides ◽  
Tmv Strains

Experimental data for determining a) the amino acid sequences of eight tryptic peptides containing 95 amino acids and b) the order of the tryptic peptides are given. Combining the data of this and of a previous paper the complete amino acid sequence of the coat protein of the TMV strain Holmes rib grass (HRG) is established (Fig. 5). It is compared with three other TMV strains the sequences of which have been determined before (Fig. 6).Differences and similarities between the sequences of the four TMV strains are discussed. HRG has a deletion of two amino acids and it is the most distantly related of the four TMV strains. When the sequence of HRG is compared to that of any of the other strains it turns out that in each case more than 50% of the 156 positions contain different amino acids (Fig. 7).The number of positions with the same amino acid in all strains and mutants so far studied is 30 per cent. These positions are not randomly distributed but clustered mainly in two regions. This finding probably reflects the restriction of amino acid exchanges by the spatial structure of the viral rod.

scholarly journals Cloning, Sequencing, and Characterization of the Iturin A Operon

2001 ◽  
Vol 183 (21) ◽  
pp. 6265-6273 ◽  
Author(s):  
Kenji Tsuge ◽  
Takanori Akiyama ◽  
Makoto Shoda
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Fatty Acid Synthetase ◽  
Amino Acid Sequences ◽  
Open Reading Frames ◽  
Upstream Sequence ◽  
Flanking Sequence ◽  
Coding Region ◽  
Iturin A ◽  
Peptide Synthetases

ABSTRACT Bacillus subtilis RB14 is a producer of the antifungal lipopeptide iturin A. Using a transposon, we identified and cloned the iturin A synthetase operon of RB14, and the sequence of this operon was also determined. The iturin A operon spans a region that is more than 38 kb long and is composed of four open reading frames, ituD, ituA, ituB, and ituC. The ituD gene encodes a putative malonyl coenzyme A transacylase, whose disruption results in a specific deficiency in iturin A production. The second gene, ituA, encodes a 449-kDa protein that has three functional modules homologous to fatty acid synthetase, amino acid transferase, and peptide synthetase. The third gene, ituB, and the fourth gene, ituC, encode 609- and 297-kDa peptide synthetases that harbor four and two amino acid modules, respectively. Mycosubtilin, which is produced by B. subtilis ATCC 6633, has almost the same structure as iturin A, but the amino acids at positions 6 and 7 in the mycosubtilin sequence ared-Ser→l-Asn, while in iturin A these amino acids are inverted (i.e., d-Asn→l-Ser). Comparison of the amino acid sequences encoded by the iturin A operon and the mycosubtilin operon revealed that ituD, ituA, andituB have high levels of homology to the counterpart genesfenF (79%), mycA (79%), and mycB(79%), respectively. Although the overall level of homology of the amino acid sequences encoded by ituC andmycC, the counterpart of ituC, is relatively low (64%), which indicates that there is a difference in the amino acid sequences of the two lipopeptides, the levels of homology between the putative serine adenylation domains and between the asparagine adenylation domains in the two synthetases are high (79 and 80%, respectively), implying that there is an intragenic domain change in the synthetases. The fact that the flanking sequence of the iturin A synthetase coding region was highly homologous to the flanking sequence that of xynD of B. subtilis 168 and the fact that the promoter of the iturin A operon which we identified was also conserved in an upstream sequence of xynD imply that horizontal transfer of this operon occurred. When the promoter was replaced by the repU promoter of the plasmid pUB110 replication protein, production of iturin A increased threefold.

scholarly journals The resistant ability to weevils and the characteristics of VrPDF1 gene of some mungbean cultivars (Vigna radiata L.Wilczek)

2016 ◽  
Vol 14 (1) ◽  
pp. 105-113
Author(s):  
Hoàng Thị Thao ◽  
Hồ Mạnh Tường ◽  
Nguyễn Thị Ngọc Lan ◽  
Nguyễn Vũ Thanh Thanh ◽  
Nguyễn Văn Sơn ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Nucleotide Sequence ◽  
Amylase Activity ◽  
Amino Acid Sequences ◽  
Coding Region ◽  
Transformation Vector ◽  
Plant Defensins ◽  
Intron Region ◽  
Comparative Results

Plant defensins play a role against the seed-feeding insects. Defensin associates with the center of α-amylase activity in the gut of weevils, thus inhibiting the digestion of starch by weevils. In this study, the resistance of eight mungbean cultivars to weevils was evaluated by the method of artificial weevils infection. The Tam TH cultivar had lowest index of susceptibility to weevils (634.63) and DX22 cultivar had highest index (1058.72), and the highest resistance to weevils was found in Tam TH and DX22 was found to have the lowest resistance. VrPDF1 genes isolated from mungbean cultivars are 356 bp in length with two exons interrupted by an intron. The coding region of the VrPDF1 gene is 228 bp in length, encoding 75 amino acids. The comparative results of the nucleotide sequence of cDNA between Tam TH  and DX22 showed that there was a difference in 13 nucleotides and comparison of amino acid sequences of the deduced protein indicated that there was a difference in 9 amino acids. Within the intron region of the VrPDF1 genes there was difference in 5 nucleotides. The genetic distance based on nucleotide sequences of the coding region of VrPDF1 gene of DX22 and seven other mungbean cultivars is 6.2% and based on the amino acid sequence deduced is 7.7%. The coding region of the VrPDF1 gene of DX22 was used to create a transformation vector aimed at creating weevil-resistant transgenic mungbean.

scholarly journals Complete chloroplast genome of Oryza sativa L. (B810s) and its phylogenetic analysis

2021 ◽  
pp. 895-901
Author(s):  
Kebao Song ◽  
Congtian Wang ◽  
Zhongbo Li ◽  
Peng Ning
Keyword(s):  
Amino Acids ◽  
Phylogenetic Analysis ◽  
Oryza Sativa ◽  
Gene Annotation ◽  
Oryza Sativa L ◽  
Amino Acid Sequences ◽  
Coding Region ◽  
Protein Coding ◽  
Cp Genome ◽  
Rna Genes

The complete chloroplast (cp) genome of Oryza sativa L.(B810S) was 134546 bp in length in the study, which contains 149 genes including 99 coding protein genes, 41 transfer RNA genes, 8 ribosomal RNA genes and 1 non-coding region by gene annotation. A total of 20879 amino acids were encoded by this cp genome, TTT (Phe) and TTG (Leu) codon were the most frequent amino acids, whereas the ACC (Thr), GCC (Ala), CTC (Leu), and AAC (Asn) codon were the least frequent ones. The content of the four bases on the cp genome were 30.6% for A, 30.4% for T, 19.4% for C and 19.6% for G, respectively. Obviously, the A+T (61.0%) content is more higher than G+C (39.0%). The gene order and content are the same as those of previously reported cp genome of Rice. Phylogenetic analysis was implemented based on concatenated amino acid sequences of 99 protein-coding genes using Neighbor-Joining method (NJ) method. Therefore, the complete B810S cp genome provides interesting insights and valuable information that can be used to identify related species and reconstruct its phylogeny. Bangladesh J. Bot. 50(3): 895-901, 2021 (September) Special

scholarly journals Molecular characterization of CDC42, a Saccharomyces cerevisiae gene involved in the development of cell polarity.

1990 ◽  
Vol 111 (1) ◽  
pp. 143-152 ◽  
Author(s):  
D I Johnson ◽  
J R Pringle
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Amino Acids ◽  
Amino Acid ◽  
Biochemical Properties ◽  
Amino Acid Sequences ◽  
Temperature Sensitive ◽  
Restrictive Temperature ◽  
Rho Proteins ◽  
Coding Region ◽  
High Degree

The Saccharomyces cerevisiae CDC42 gene product is involved in the morphogenetic events of the cell division cycle; temperature-sensitive cdc42 mutants are unable to form buds and display delocalized cell-surface deposition at the restrictive temperature (Adams, A. E. M., D. I. Johnson, R. M. Longnecker, B. F. Sloat, and J. R. Pringle. 1990. J. Cell Biol. 111:131-142). To begin a molecular analysis of CDC42 function, we have isolated the CDC42 gene from a yeast genomic DNA library. The use of the cloned DNA to create a deletion of CDC42 confirmed that the gene is essential. Overexpression of CDC42 under control of the GAL10 promoter was not grossly deleterious to cell growth but did perturb the normal pattern of selection of budding sites. Determination of the DNA and predicted amino acid sequences of CDC42 revealed a high degree of similarity in amino acid sequence to the ras and rho (Madaule, P., R. Axel, and A. M. Myers. 1987. Proc. Natl. Acad. Sci. 84:779-783) families of gene products. The similarities to ras proteins (approximately 40% identical or related amino acids overall) were most pronounced in the regions that have been implicated in GTP binding and hydrolysis and in the COOH-terminal modifications leading to membrane association, suggesting that CDC42 function also involves these biochemical properties. The similarities to the rho proteins (approximately 60% identical or related amino acids overall) were more widely distributed through the coding region, suggesting more extensive similarities in as yet undefined biochemical properties and functions.

scholarly journals Molecular Cloning and Bioinformatics Analysis of DQA Gene from Mink (Neovison vison)

2019 ◽  
Vol 20 (5) ◽  
pp. 1037
Author(s):  
Zhaobin Fan ◽  
Houfeng Zhang ◽  
Min Rong ◽  
Dongmei Meng ◽  
Zhenxing Yu ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Molecular Mechanisms ◽  
Signal Sequence ◽  
Amino Acid Sequences ◽  
Neovison Vison ◽  
Random Coil ◽  
Amino Acid Residues ◽  
Coding Region ◽  
Full Length Sequence

In the present study, we cloned, sequenced, and explored the structural and functional characteristics of the major histocompatibility complex (MHC)-DQA gene from mink (Neovison vison) for the first time. The full-length sequence of DQA gene was 1147-bp-long, contained a coding region of 768-bp, which was predicted to encoding 255 amino acid residues. The comparison between DQA from mink (Neovison vison) and other MHC-DQA molecules from different animal species showed that nucleotide and encoded amino acid sequences of the mink DQA gene exhibited high similarity with the ferret (Mustela pulourius furo). Phylogenetic analysis revealed that mink (Neovison vison) DQA is grouped with that of ferret (Mustela pulourius furo). The cloned sequence contained a 23-amino acid NH2-terminal signal sequence with the signal peptide cutting site located in amino acids 23–24, and had three Asn-Xaa-Ser/Thr sequons. Three cysteine residues were also identified (Cys-85, Cys-121, and Cys-138). The 218 to 240 amino acids were predicted to be the transmembrane domains. The prediction of the secondary structure revealed three α-helixes and fourteen β-sheets in Neovison vison DQA protein, while random coil was a major pattern. In this study, the whole CDS sequence of Neovison vison DQA gene was successfully cloned, which was valuable for exploring the function and antiviral molecular mechanisms underlying the molecule. The findings of the present study have laid the foundation for the disease resistance and breeding of mink.

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