scholarly journals Genomic Organization in the Amino Acid Coding Sequence of Equine CYP17 Gene.

2000 ◽  
Vol 11 (4) ◽  
pp. 99-105
Author(s):  
Telhisa HASEGAWA ◽  
Fumio SATO ◽  
Nobushige ISHIDA
Keyword(s):  
Amino Acid ◽  
Genomic Organization ◽  
Coding Sequence ◽  
Cyp17 Gene

scholarly journals Amino Acid Repeats Cause Extraordinary Coding Sequence Variation in the Social Amoeba Dictyostelium discoideum

PLoS ONE ◽  
2012 ◽  
Vol 7 (9) ◽  
pp. e46150 ◽  
Author(s):  
Clea Scala ◽  
Xiangjun Tian ◽  
Natasha J. Mehdiabadi ◽  
Margaret H. Smith ◽  
Gerda Saxer ◽  
...  
Keyword(s):  
Amino Acid ◽  
Dictyostelium Discoideum ◽  
Sequence Variation ◽  
Social Amoeba ◽  
Coding Sequence ◽  
Amino Acid Repeats ◽  
The Social

scholarly journals Different translation dynamics of β-and γ-actin regulates cell migration

eLife ◽  
2021 ◽  
Vol 10 ◽  
Author(s):  
Pavan Vedula ◽  
Satoshi Kurosaka ◽  
Brittany MacTaggart ◽  
Qin Ni ◽  
Garegin Papoian ◽  
...  
Keyword(s):  
Cell Migration ◽  
Amino Acid ◽  
Single Molecule ◽  
Amino Acid Level ◽  
Focal Adhesions ◽  
Mesenchymal Cell ◽  
Cell Periphery ◽  
Pronounced Difference ◽  
Coding Sequence

β- and γ-cytoplasmic actins are ubiquitously expressed in every cell type and are nearly identical at the amino acid level but play vastly different roles in vivo. Their essential roles in embryogenesis and mesenchymal cell migration critically depend on the nucleotide sequences of their genes, rather than their amino acid sequence, however it is unclear which gene elements underlie this effect. Here we address the specific role of the coding sequence in β- and γ-cytoplasmic actins' intracellular functions, using stable polyclonal populations of immortalized mouse embryonic fibroblasts with exogenously expressed actin isoforms and their 'codon-switched' variants. When targeted to the cell periphery using the β-actin 3′UTR, β-actin and γ-actin have differential effects on cell migration. These effects directly depend on the coding sequence. Single molecule measurements of actin isoform translation, combined with fluorescence recovery after photobleaching, demonstrate a pronounced difference in β- and γ-actins' translation elongation rates in cells, leading to changes in their dynamics at the focal adhesions, impairments in actin bundle formation, and reduced cell anchoring to the substrate during migration. Our results demonstrate that coding sequence-mediated differences in actin translation play a key role in cell migration.

Polymorphism in the coding sequence of the horse transferrin gene

Genome ◽  
1994 ◽  
Vol 37 (1) ◽  
pp. 157-165 ◽  
Author(s):  
Margaret A. Carpenter ◽  
Tom E. Broad
Keyword(s):  
Amino Acid ◽  
Iron Transport ◽  
Nucleotide Substitution ◽  
Three Dimensional ◽  
Sequence Polymorphism ◽  
Dimensional Structure ◽  
Amino Acid Substitutions ◽  
Nucleotide Substitutions ◽  
Coding Sequence ◽  
Transferrin Gene

Transferrin, the iron transport protein of the blood, is highly polymorphic in many species, including the horse. A number of sequence polymorphisms that distinguish several of the variants of horse transferrin are reported here. Previous studies indicated that exons 12 and 15 were likely to be polymorphic. Sequencing regions of exons 12 and 15 from D and R variants revealed 10 nucleotide substitutions that encoded six amino acid replacements. The F1, F2, H2, and * variants were identical to D, and the O variant was almost identical to R, in the regions studied. The data indicated that the horse transferrin variants make up two distinct groups. The positions of differences between the D and F1 alleles were determined by analyzing single-stranded conformation polymorphisms. Sequencing then revealed three nucleotide substitutions, two of which encoded amino acid substitutions. Location of the eight polymorphic residues on the three-dimensional structure of human lactoferrin revealed that all were clustered at one end of the C-lobe.Key words: sequence polymorphism, transferrin, horse, nucleotide substitution, allele.

scholarly journals PF15p Is the Chlamydomonas Homologue of the Katanin p80 Subunit and Is Required for Assembly of Flagellar Central Microtubules

2004 ◽  
Vol 3 (4) ◽  
pp. 870-879 ◽  
Author(s):  
Erin E. Dymek ◽  
Paul A. Lefebvre ◽  
Elizabeth F. Smith
Keyword(s):  
Amino Acid ◽  
Significant Role ◽  
Insertional Mutagenesis ◽  
Flagellar Motility ◽  
Wild Type ◽  
Central Pair ◽  
Coding Sequence ◽  
Microtubule Severing ◽  
Central Apparatus

ABSTRACT Numerous studies have indicated that the central apparatus plays a significant role in regulating flagellar motility, yet little is known about how the central pair of microtubules or their associated projections assemble. Several Chlamydomonas mutants are defective in central apparatus assembly. For example, mutant pf15 cells have paralyzed flagella that completely lack the central pair of microtubules. We have cloned the wild-type PF15 gene and confirmed its identity by rescuing the motility and ultrastructural defects in two pf15 alleles, the original pf15a mutant and a mutant generated by insertional mutagenesis. Database searches using the 798-amino-acid polypeptide predicted from the complete coding sequence indicate that the PF15 gene encodes the Chlamydomonas homologue of the katanin p80 subunit. Katanin was originally identified as a heterodimeric protein with a microtubule-severing activity. These results reveal a novel role for the katanin p80 subunit in the assembly and/or stability of the central pair of flagellar microtubules.

scholarly journals Interstrain Variation in the Human Cytomegalovirus DNA Polymerase Sequence and Its Effect on Genotypic Diagnosis of Antiviral Drug Resistance

1999 ◽  
Vol 43 (6) ◽  
pp. 1500-1502 ◽  
Author(s):  
Sunwen Chou ◽  
Nell S. Lurain ◽  
Adriana Weinberg ◽  
Guang-Yung Cai ◽  
Prem L. Sharma ◽  
...  
Keyword(s):  
Drug Resistance ◽  
Amino Acid ◽  
Dna Polymerase ◽  
Human Cytomegalovirus ◽  
Antiviral Drug ◽  
Resistance Mutations ◽  
Sequence Alignments ◽  
Coding Sequence ◽  
Antiviral Drug Resistance ◽  
Almost All

ABSTRACT The polymerase (pol) coding sequence was determined for 40 independent clinical cytomegalovirus isolates sensitive to ganciclovir and foscarnet. Sequence alignments showed >98% interstrain homology and amino acid variation in only 4% of the 1,237 codons. Almost all variation occurred outside of conserved functional domains where resistance mutations have been identified.

Genomic organization of the human excitatory amino acid transporter gene GLT-1

Neuroreport ◽  
1997 ◽  
Vol 8 (3) ◽  
pp. 775-777 ◽  
Author(s):  
Thomas Meyer ◽  
Albert C. Ludolph ◽  
Markus Morkel ◽  
Christian Hagemeier ◽  
Astrid Speer
Keyword(s):  
Amino Acid ◽  
Genomic Organization ◽  
Excitatory Amino Acid ◽  
Amino Acid Transporter ◽  
Transporter Gene ◽  
Excitatory Amino Acid Transporter ◽  
Acid Transporter ◽  
Amino Acid Transporter Gene

scholarly journals Molecular Characterization of an Avian Astrovirus

2000 ◽  
Vol 74 (13) ◽  
pp. 6173-6177 ◽  
Author(s):  
Matthew D. Koci ◽  
Bruce S. Seal ◽  
Stacey Schultz-Cherry
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence ◽  
Animal Species ◽  
Genomic Organization ◽  
Predicted Amino Acid Sequence ◽  
Enteric Disease ◽  
Nucleotide Level ◽  
Human Astroviruses

ABSTRACT Astroviruses are known to cause enteric disease in several animal species, including turkeys. However, only human astroviruses have been well characterized at the nucleotide level. Herein we report the nucleotide sequence, genomic organization, and predicted amino acid sequence of a turkey astrovirus isolated from poults with an emerging enteric disease.

Predicted amino acid sequence and genomic organization of Trypanosoma cruzi hsp 60 genes

1993 ◽  
Vol 58 (1) ◽  
pp. 25-31 ◽  
Author(s):  
Marcia Giambiagi-de Marval ◽  
Keith Gottesdiener ◽  
Edson Rondinelli ◽  
Lex H.T. Van der Ploeg
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Trypanosoma Cruzi ◽  
Genomic Organization ◽  
Predicted Amino Acid Sequence
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