Nucleotide sequence of the carboxy-terminal portion of a lodgepole pine actin gene

1988 ◽  
Vol 18 (12) ◽  
pp. 1595-1602 ◽  
Author(s):  
J. R. Kenny ◽  
B. P. Dancik ◽  
L. Z. Florence ◽  
F. E. Nargang
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Intron Position ◽  
Amino Acid Sequences ◽  
Pairwise Comparisons ◽  
Actin Gene ◽  
Terminal Portion ◽  
The Third ◽  
Actin Genes ◽  
Carboxy Terminal

We have determined the nucleotide sequence of the carboxy-terminal portion of an actin gene (PAc1-A) isolated from Pinuscontorta var. latifolia (Engelm.). Pairwise comparisons of both nucleotide and deduced amino acid sequences were made among PAc1-A, the soybean actins SAc3 and SAc1, maize actin MAc1, chicken β-actin, and yeast β-actin. Of the other actins SAc3 was most similar to the PAc1-A amino acid sequence (91.3% identity) and yeast actin the least similar (78.3% identity). The intron in PAc1-A is present at the same location as the third intron found in MAc1, SAc1, and SAc3 actin genes. This conservation of intron position is unusual when compared with nonplant actin genes.

scholarly journals THE MOLECULAR EVOLUTION OF ACTIN

Genetics ◽  
1986 ◽  
Vol 114 (1) ◽  
pp. 315-332
Author(s):  
Robin C Hightower ◽  
Richard B Meagher
Keyword(s):  
Amino Acid ◽  
Molecular Evolution ◽  
Gene Family ◽  
Amino Acid Sequences ◽  
Actin Gene ◽  
Muscle Actin ◽  
Gene Sequences ◽  
Actin Genes ◽  
Cytoplasmic Actin ◽  
Replacement Substitution

ABSTRACT We have investigated the molecular evolution of plant and nonplant actin genes comparing nucleotide and amino acid sequences of 20 actin genes. Nucleotide changes resulting in amino acid substitutions (replacement substitutions) ranged from 3-7% for all pairwise comparisons of animal actin genes with the following exceptions. Comparisons between higher animal muscle actin gene sequences and comparisons between higher animal cytoplasmic actin gene sequences indicated <3% divergence. Comparisons between plant and nonplant actin genes revealed, with two exceptions, 11-15% replacement substitution. In the analysis of plant actins, replacement substitution between soybean actin genes SAc1, SAc3, SAc4 and maize actin gene MAc1 ranged from 8-10%, whereas these members within the soybean actin gene family ranged from 6-9% replacement substitution. The rate of sequence divergence of plant actin sequences appears to be similar to that observed for animal actins. Furthermore, these and other data suggest that the plant actin gene family is ancient and that the families of soybean and maize actin genes have diverged from a single common ancestral plant actin gene that originated long before the divergence of monocots and dicots. The soybean actin multigene family encodes at least three classes of actin. These classes each contain a pair of actin genes that have been designated kappa (SAc1, SAc6), lambda (SAc2, SAc4) and mu (SAc3, SAc7). The three classes of soybean actin are more divergent in nucleotide sequence from one another than higher animal cytoplasmic actin is divergent from muscle actin. The location and distribution of amino acid changes were compared between actin proteins from all sources. A comparison of the hydropathy of all actin sequences, except from Oxytricha, indicated a strong similarity in hydropathic character between all plant and nonplant actins despite the greater number of replacement substitutions in plant actins. These protein sequence comparisons are discussed with respect to the demonstrated and implicated roles of actin in plants and animals, as well as the tissue-specific expression of actin.

Structure of a human smooth muscle actin gene (aortic type) with a unique intron site

1984 ◽  
Vol 4 (6) ◽  
pp. 1073-1078
Author(s):  
H Ueyama ◽  
H Hamada ◽  
N Battula ◽  
T Kakunaga
Keyword(s):  
Smooth Muscle ◽  
Amino Acid ◽  
Smooth Muscle Actin ◽  
Amino Acid Sequences ◽  
Actin Gene ◽  
Muscle Actin ◽  
Aortic Smooth Muscle ◽  
Actin Genes ◽  
Muscle Actin Gene ◽  
Normal Human

A recombinant phage containing an actin gene (lambda Ha201) was isolated from a human DNA library and the structure of the actin gene was determined. The amino acid sequences deduced from the nucleotide sequences of lambda Ha201 were compared with those of six actin isoforms; they matched those of bovine aortic smooth muscle actin, except for codon 309, which was valine (GTC) in lambda Ha201 and alanine (GCN) in bovine aortic smooth muscle actin. Southern blot hybridization experiments showed that the gene of normal human cells did not have the TaqI-sensitive site around position 309, whereas half of the genes of HUT14 cells did. These results indicate that one allele of the aortic smooth muscle actin gene in HUT14 cells has a transition point mutation (C----T) at codon 309 and that the amino acid sequences of normal human aorta and bovine smooth muscle actins are probably identical. In addition to the five introns interrupting exons at codons 150, 204, and 267, and between codons 41 and 42 and 327 and 328, which are common to skeletal muscle and cardiac muscle actin genes, the smooth muscle actin gene has two more intron sites between codons 84 and 85 and 121 and 122. The previously unreported intron site between codons 84 and 85 is unique to the smooth muscle actin gene. The intron site between codons 121 and 122 is common to beta-actin genes but is not found in other muscle actin genes. A hypothesis is proposed for the evolutionary pathway of the actin gene family.

scholarly journals Structure of a human smooth muscle actin gene (aortic type) with a unique intron site.

1984 ◽  
Vol 4 (6) ◽  
pp. 1073-1078 ◽  
Author(s):  
H Ueyama ◽  
H Hamada ◽  
N Battula ◽  
T Kakunaga
Keyword(s):  
Smooth Muscle ◽  
Amino Acid ◽  
Smooth Muscle Actin ◽  
Amino Acid Sequences ◽  
Actin Gene ◽  
Muscle Actin ◽  
Aortic Smooth Muscle ◽  
Actin Genes ◽  
Muscle Actin Gene ◽  
Normal Human

A recombinant phage containing an actin gene (lambda Ha201) was isolated from a human DNA library and the structure of the actin gene was determined. The amino acid sequences deduced from the nucleotide sequences of lambda Ha201 were compared with those of six actin isoforms; they matched those of bovine aortic smooth muscle actin, except for codon 309, which was valine (GTC) in lambda Ha201 and alanine (GCN) in bovine aortic smooth muscle actin. Southern blot hybridization experiments showed that the gene of normal human cells did not have the TaqI-sensitive site around position 309, whereas half of the genes of HUT14 cells did. These results indicate that one allele of the aortic smooth muscle actin gene in HUT14 cells has a transition point mutation (C----T) at codon 309 and that the amino acid sequences of normal human aorta and bovine smooth muscle actins are probably identical. In addition to the five introns interrupting exons at codons 150, 204, and 267, and between codons 41 and 42 and 327 and 328, which are common to skeletal muscle and cardiac muscle actin genes, the smooth muscle actin gene has two more intron sites between codons 84 and 85 and 121 and 122. The previously unreported intron site between codons 84 and 85 is unique to the smooth muscle actin gene. The intron site between codons 121 and 122 is common to beta-actin genes but is not found in other muscle actin genes. A hypothesis is proposed for the evolutionary pathway of the actin gene family.

scholarly journals A novel giant secretion polypeptide in Chironomus salivary glands: implications for another Balbiani ring gene.

1985 ◽  
Vol 101 (3) ◽  
pp. 1044-1051 ◽  
Author(s):  
W Y Kao ◽  
S T Case
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Salivary Glands ◽  
Cyanogen Bromide ◽  
Tryptic Peptide ◽  
Amino Acid Sequences ◽  
The Other ◽  
Balbiani Ring ◽  
Sequence Organization ◽  
Peptide Maps

Chironomus salivary glands contain a family of high Mr (approximately 1,000 X 10(3)) secretion polypeptides thought to consist of three components: sp-Ia, sp-Ib, and sp-Ic. The use of a new extraction protocol revealed a novel high Mr component, sp-Id. Results of a survey of individual salivary glands indicated that sp-Id was widespread in more than a dozen strains of C. tentans and C. pallidivittatus. Sp-Id was phosphorylated at Ser residues, and a comparison of cyanogen bromide and tryptic peptide maps of 32P-labeled polypeptides suggested that sp-Ia, sp-Ib, and sp-Id are comprised of similar but nonidentical tandemly repeated amino acid sequences. We concluded that sp-Id is encoded by an mRNA whose size and nucleotide sequence organization are similar to Balbiani ring (BR) mRNAs that code for the other sp-I components. Furthermore, parallel repression of sp-Ib and sp-Id synthesis by galactose led us to hypothesize that both of their genes exist within Balbiani ring 2.

scholarly journals Potential Selection of LMP1 Variants in Nasopharyngeal Carcinoma

2004 ◽  
Vol 78 (2) ◽  
pp. 868-881 ◽  
Author(s):  
Rachel H. Edwards ◽  
Diane Sitki-Green ◽  
Dominic T. Moore ◽  
Nancy Raab-Traub
Keyword(s):  
Amino Acid ◽  
Cytotoxic T Lymphocyte ◽  
Amino Acid Sequences ◽  
Barr Virus ◽  
Distinct Sequence ◽  
Epstein Barr ◽  
Virus Latent Membrane Protein ◽  
Multiple Strains ◽  
Carboxy Terminal ◽  
Selection Of

ABSTRACT Seven distinct sequence variants of the Epstein-Barr virus latent membrane protein 1 (LMP1) have been identified by distinguishing amino acid changes in the carboxy-terminal domain. In this study the transmembrane domains are shown to segregate identically with the distinct carboxy-terminal amino acid sequences. Since strains of LMP1 have been shown to differ in abundance between blood and throat washes, nasopharyngeal carcinomas (NPCs) from areas of endemicity and nonendemicity with matching blood were analyzed by using a heteroduplex tracking assay to distinguish LMP1 variants. Striking differences were found between the compartments with the Ch1 strain prevalent in the NPCs from areas of endemicity and nonendemicity and the B958 strain prevalent in the blood of the endemic samples, whereas multiple strains of LMP1 were prevalent in the blood of the nonendemic samples. The possible selection against the B958 strain appearing in the tumor was highly significant (P < 0.0001). Sequence analysis of the full-length LMP1 variants revealed changes in many of the known and computer-predicted HLA-restricted epitopes with changes in key positions in multiple, potential epitopes for the specific HLA of the patients. These amino acid substitutions at key positions in the LMP1 epitopes may result in a reduced cytotoxic-T-lymphocyte response. These data indicate that strains with specific variants of LMP1 are more likely to be found in NPC. The predominance of specific LMP1 variants in NPC could reflect differences in the biologic or molecular properties of the distinct forms of LMP1 or possible immune selection.

scholarly journals Taxonomic status of Bhanja and Kismayo viruses (family Bunyaviridae)

2012 ◽  
Vol 17 (4) ◽  
pp. 4-8
Author(s):  
A. S Klimentov ◽  
A. P Gmyl ◽  
A. M Butenko ◽  
L. V Gmyl ◽  
O. V Isaeva ◽  
...  
Keyword(s):  
Phylogenetic Analysis ◽  
Amino Acid ◽  
Nucleotide Sequence ◽  
Taxonomic Status ◽  
Amino Acid Sequences ◽  
The Family ◽  
L Segment

The nucleotide sequence of M= (1398 nucleotides and L= (6186 nucleotides) segments of the genome of Bhanja virus and L-segment (1297 nucleotides) of Kismayo virus has been partially determined. Phylogenetic analysis of deduced amino acid sequences showed that these viruses are novel members of the Flebovirus (Phlebovirus) genus in the family Bunyaviridae

Predicted structure of the bovine calcitonin gene-related peptide and the carboxy-terminal flanking peptide of bovine calcitonin precursor

1991 ◽  
Vol 6 (2) ◽  
pp. 147-152 ◽  
Author(s):  
K. Collyear ◽  
S. I. Girgis ◽  
G. Saunders ◽  
I. MacIntyre ◽  
G. Holt
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Nucleotide Sequence ◽  
Genomic Library ◽  
Amino Acid Peptide ◽  
Related Peptide ◽  
Calcitonin Gene ◽  
Significant Homology ◽  
Human Counterpart ◽  
Carboxy Terminal

ABSTRACT We have isolated from a bovine genomic library a clone which contains the calcitonin (CT) and CT gene-related peptide (CGRP) sequences, using probes representing the human CT and CGRP sequences. Sequence analysis has identified the nucleotide sequence coding for bovine CT, its C-terminal flanking peptide and bovine CGRP. The deduced amino acid sequence of bovine CGRP revealed a significant homology with other CGRPs so far reported. It differs by only one amino acid from rat CGRPα and porcine CGRP, and by three and four amino acids from human CGRPβ and α respectively. Bovine CT has, however, only 14 out of 32 residues in common with human CT. As in the human CT precursor, the C-terminal flanking peptide of bovine CT precursor is a 21 amino acid peptide. It shares only 11 residues in common with its human counterpart. This study thus provides further evidence that CGRP, in contrast to CT and its C-terminal flanking peptide, is a highly conserved molecule.

A head-activator binding protein is present in hydra in a soluble and a membrane-anchored form

Development ◽  
1999 ◽  
Vol 126 (18) ◽  
pp. 4077-4086 ◽  
Author(s):  
W. Hampe ◽  
J. Urny ◽  
I. Franke ◽  
S.A. Hoffmeister-Ullerich ◽  
D. Herrmann ◽  
...  
Keyword(s):  
Stem Cells ◽  
Amino Acid ◽  
Transmembrane Domain ◽  
Binding Protein ◽  
Amino Acid Sequences ◽  
Secreted Protein ◽  
Specific Antibodies ◽  
Head Activator ◽  
Carboxy Terminal

The neuropeptide head activator plays an important role for proliferation and determination of stem cells in hydra. By affinity chromatography a 200 kDa head-activator binding protein, HAB, was isolated from the multiheaded mutant of Chlorohydra viridissima. Partial amino acid sequences were used to clone the HAB cDNA which coded for a receptor with a unique alignment of extracellular modules, a transmembrane domain, and a short carboxy-terminal cytoplasmic tail. A mammalian HAB homologue with identical alignment of these modules is expressed early in brain development. Specific antibodies revealed the presence of HAB in hydra as a transmembrane receptor, but also as secreted protein, both capable of binding head activator. Secretion of HAB during regeneration and expression in regions of high determination potential hint at a role for HAB in regulating the concentration and range of action of head activator.

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 Structural gene and complete amino acid sequence of Vibrio alginolyticus collagenase

1992 ◽  
Vol 281 (3) ◽  
pp. 703-708 ◽  
Author(s):  
H Takeuchi ◽  
Y Shibano ◽  
K Morihara ◽  
J Fukushima ◽  
S Inami ◽  
...  
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence ◽  
Structural Gene ◽  
Sequence Similarity ◽  
Vibrio Alginolyticus ◽  
Amino Acid Sequences ◽  
Dna Encoding ◽  
Cloned Gene ◽  
Collagenase Gene

The DNA encoding the collagenase of Vibrio alginolyticus was cloned, and its complete nucleotide sequence was determined. When the cloned gene was ligated to pUC18, the Escherichia coli expression vector, bacteria carrying the gene exhibited both collagenase antigen and collagenase activity. The open reading frame from the ATG initiation codon was 2442 bp in length for the collagenase structural gene. The amino acid sequence, deduced from the nucleotide sequence, revealed that the mature collagenase consists of 739 amino acids with an Mr of 81875. The amino acid sequences of 20 polypeptide fragments were completely identical with the deduced amino acid sequences of the collagenase gene. The amino acid composition predicted from the DNA sequence was similar to the chemically determined composition of purified collagenase reported previously. The analyses of both the DNA and amino acid sequences of the collagenase gene were rigorously performed, but we could not detect any significant sequence similarity to other collagenases.

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