scholarly journals Lack of correlation between dysgenic traits in the hobo system of hybrid dysgenesis in Drosophila melanogaster

1996 ◽  
Vol 67 (3) ◽  
pp. 219-226 ◽  
Author(s):  
C. Bazin ◽  
D. Higuet
Keyword(s):  
Drosophila Melanogaster ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Molecular Analysis ◽  
Restriction Fragment ◽  
The Other ◽  
Hybrid Dysgenesis ◽  
Full Size ◽  
Gonadal Atrophy ◽  
Different Strains

SummaryCurrently in the hobo system of hybrid dysgenesis, strain classification is based on the presence/absence of the 2·6 kb Xho I restriction fragment. Using this criterion, strains are classified as: (1) H strains when full-size elements are detected by presence of a 2·6 kb Xho I restriction fragment; they can also contain internally deleted elements; (2) DH strains when only deleted elements are detected (Xho I restriction fragment less than 2·6 kb); (3) E strains, devoid of any restriction fragment equal to or less than 2·6 kb in length. In addition, the strains can be classified on their ability to generate gonadal atrophy (GD sterility) when males of a studied strain are crossed with females from an E strain (dysgenic cross). Here we try to define the nature of the dysgenic cross, which leads us to analyse the different components of the dysgenic syndrome and to look for eventual correlations between them. Molecular analysis, GD sterility tests, hobo mobilization with the haw strain and the vgal strain, and hereditary transmission of the instability at the vg locus have been assayed in different strains. We show that the occurrence of GD sterility depends on the tested H strains as expected, but also on the E strains used. On the other hand we do not find any correlation between the different dysgenic parameters. Our data reveal that molecular and GD sterility tests are not sufficient to classify strains in the hobo system, and that all the components of the dysgenic syndrome must be taken into account. Our results are discussed with regard to active and full-size elements in relation to the structure of the S region where an amino acid sequence (TPE) presents a repetition polymorphism

C-Terminal amino acid sequence of chicken pepsinogen and its homology with sequences of other acid proteases

1980 ◽  
Vol 45 (4) ◽  
pp. 1144-1154 ◽  
Author(s):  
Miroslav Baudyš ◽  
Helena Keilová ◽  
Vladimír Kostka
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
The Other ◽  
Terminal Sequence ◽  
Terminal Part ◽  
Terminal Amino Acid ◽  
Tryptic Peptides ◽  
Terminal Amino ◽  
High Degree ◽  
Terminal Amino Acid Sequence

To determine the primary structure of the C-terminal part of the molecule of chicken pepsinogen the tryptic, chymotryptic and thermolytic digest of the protein were investigated and peptides derived from this region were sought. These peptides permitted the following 21-residue C-terminal sequence to be determined: ...Ile-Arg-Glu-Tyr-Tyr-Val-Ile-Phe-Asp-Arg-Ala-Asn-Asn-Lys-Val-Gly-Leu-Ser-Pro-Leu-Ser.COOH. A comparison of this structure with the C-terminal sequential regions of the other acid proteases shows a high degree of homology between chicken pepsinogen and these proteases (e.g., the degree of homology with respect to hog pepsinogen and calf prochymosin is about 66%). Additional tryptic peptides, derived from the N-terminal part of the zymogen molecule whose amino acid sequence has been reported before, were also obtained in this study. This sequence was extended by two residues using an overlapping peptide. An ancillary result of this study was the isolation of tryptic peptides derived from other regions of the zymogen molecule.

scholarly journals The complete amino acid sequence of three alcohol dehydrogenase alleloenzymes (AdhN-11, AdhS and AdhUF) from the fruitfly Drosophila melanogaster

1980 ◽  
Vol 187 (3) ◽  
pp. 875-883 ◽  
Author(s):  
D R Thatcher
Keyword(s):  
Drosophila Melanogaster ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Alcohol Dehydrogenase ◽  
Aspartic Acid ◽  
Structure Prediction ◽  
Secondary Structure Prediction ◽  
British Library ◽  
Horse Liver ◽  
And Staphylococcus Aureus

The sequence of three alcohol dehydrogenase alleloenzymes from the fruitfly Drosophila melanogaster has been determined by the sequencing of peptides produced by trypsin, chymotrypsin, thermolysin, pepsin and Staphylococcus aureus-V8-proteinase digestion. The amino acid sequence shows no obvious homology with the published sequences of the horse liver and yeast enzymes, and secondary structure prediction suggests that the nucleotide-binding domain is located in the N-terminal half of the molecule. The amino acid substitutions between AdhN-11 (a point mutation of AdhF), AdhS and AdhUF alleloenzymes were identified. AdhN-11 alcohol dehydrogenase differed from the other two by a glycine-14-(AdhS and AdhUF)-to-aspartic acid substitution, the AdhS enzyme from AdhN-11 and AdhUF enzymes by a threonine-192-(AdhN-11 and AdhUF)-to-lysine (AdhS) substitution and the AdhUF enzyme was found to differ by an alanine-45-(AdhS and AdhN-11)-to-aspartic acid (AdhUF) charge substitution and a ‘silent’ asparagine-8-(AdhS and AdhN-11)-to-alanine (AdhUF) substitution. Detailed sequence evidence has been deposited as Supplementary Publication SUP 50107 (36 pages) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1978) 169, 5.

scholarly journals Genetic variability in cysteine protease genes ofHaemonchus contortus

Parasitology ◽  
2004 ◽  
Vol 128 (5) ◽  
pp. 549-559 ◽  
Author(s):  
A. RUIZ ◽  
J. M. MOLINA ◽  
A. NJUE ◽  
R. K. PRICHARD
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Genetic Variability ◽  
Amino Acid Sequence ◽  
Cysteine Protease ◽  
Haemonchus Contortus ◽  
Significant Variation ◽  
Nucleotide Diversity ◽  
Cysteine Proteases ◽  
Different Strains

To increase the existent genetic variability in cysteine proteases, a polymorphism study was performed inHaemonchus contortusby comparing 2 different strains of the parasite: North American (NA) and Spanish (SP) strains. For this purpose, the polymorphism of 5 previously reported genes (AC-1,AC-3,AC-4,AC-5andGCP-7) were analysed by PCR–SSCP and sequencing procedures. Based on the SSCP results, a total of 20 different alleles were identified for the 5lociassessed. Exceptlocus AC-5, all thelociwere polymorphic.Loci AC-1,AC-3,AC-4andGCP-7showed 5, 8, 2 and 4 alleles, respectively. The allelic frequencies ranged from 0·0070 to 0·8560 and were significantly different between strains. In addition, nucleotide diversity analyses showed a significant variation within and between strains. The variations in the nucleotide sequence of the different alleles were translated in some cases into changes in the amino acid sequence. Evidence of genetic variability in cysteine proteases from two different strains ofH. contortusfor the same set of genes had not been previously reported.

scholarly journals Arrangement of the disulphide bridges in human low-Mr kininogen

1987 ◽  
Vol 247 (1) ◽  
pp. 15-21 ◽  
Author(s):  
J Kellermann ◽  
C Thelen ◽  
F Lottspeich ◽  
A Henschen ◽  
R Vogel ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Heavy Chain ◽  
Light Chain ◽  
The Other ◽  
Critical Importance

The arrangement of the disulphide bridges in human low-Mr kininogen has been elucidated. Low-Mr kininogen contains 18 half-cystine residues forming nine disulphide bridges. The first and the last half-cystine residues of the amino acid sequence form a disulphide loop which spans the heavy- and the light-chain portion of the kininogen molecule. The other 16 half-cystine residues are linked consecutively to form eight loops of 4-20 amino acids; these loops are lined up in the heavy-chain portion of the kininogen molecule. In this way, a particular pattern of disulphide loops is formed which seems to be of critical importance for the inhibitor function of human kininogen.

scholarly journals The production and molecular properties of the zinc β-lactamase of Pseudomonas maltophilia IID 1275

1985 ◽  
Vol 229 (3) ◽  
pp. 791-797 ◽  
Author(s):  
R Bicknell ◽  
E L Emanuel ◽  
J Gagnon ◽  
S G Waley
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Thiol Group ◽  
The Other ◽  
Beta Lactamase ◽  
Beta Lactamases ◽  
Zinc Enzyme ◽  
Pseudomonas Maltophilia ◽  
Measurable Rate ◽  
Beta Lactamase Ii

The production and purification of a tetrameric zinc beta-lactamase from Pseudomonas maltophilia IID 1275 were greatly improved. Three charge variants were isolated by chromatofocusing. The subunits each contain two atomic proportions of zinc and (in two of the variants) one residue of cysteine. The thiol group is not required for activity, nor does it appear to bind to the metal. Replacement of zinc by cobalt, cadmium or nickel takes place at a measurable rate, and gives enzymes that are less active than the zinc enzyme. The properties of this enzyme differ from those of the other known zinc beta-lactamase, beta-lactamase II from Bacillus cereus. The amino acid sequence of the N-terminal 32 residues was determined; there is no similarity to the N-terminal sequences of other beta-lactamases.

scholarly journals Nucleotide Sequence of theblaRTG-2 (CARB-5) Gene and Phylogeny of a New Group of Carbenicillinases

2000 ◽  
Vol 44 (4) ◽  
pp. 1070-1074 ◽  
Author(s):  
Daniele Choury ◽  
Marie-France Szajnert ◽  
Marie-Laure Joly-Guillou ◽  
Kemal Azibi ◽  
Marc Delpech ◽  
...  
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence ◽  
Proteus Mirabilis ◽  
Acinetobacter Calcoaceticus ◽  
The Other ◽  
Separate Group ◽  
Phylogenetic Studies

ABSTRACT We determined the nucleotide sequence of the bla gene for the Acinetobacter calcoaceticus β-lactamase previously described as CARB-5. Alignment of the deduced amino acid sequence with those of known β-lactamases revealed that CARB-5 possesses an RTG triad in box VII, as described for the Proteus mirabilis GN79 enzyme, instead of the RSG consensus characteristic of the other carbenicillinases. Phylogenetic studies showed that these RTG enzymes constitute a new, separate group, possibly ancestors of the carbenicillinase family.

scholarly journals A role for the Fem-1 gene of Drosophila melanogaster in adult courtship

2020 ◽  
Author(s):  
Miles Thies ◽  
Brett Berke
Keyword(s):  
Drosophila Melanogaster ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Sex Determination ◽  
Mutational Analysis ◽  
Courtship Behavior ◽  
Evolutionary Relationships ◽  
Induced Mutations ◽  
C Elegans ◽  
Conserved Gene

The Fem family of genes influences sex determination and/or the development of sex-specific characteristics in a wide variety of organisms. Here, we describe the first mutational analysis of the Fem-1 gene of Drosophila melanogaster. The amino acid sequence of the two Drosophila Fem-1 transcripts are moderately conserved compared to that of both Fem-1 in C. elegans and the two Fem-1 transcripts in humans, with multiple ankyrin repeats. Using two transposon-induced mutations of Drosophila Fem-1, we observed striking defects in adult courtship behavior that are attributed to defects in male courting as opposed to female receptivity. Specifically, viable Fem-1 mutant males courted Fem-1 females more vigorously with an increased amount of chasing and singing than pairs of control flies. Nevertheless, Fem-1 males did not copulate at a higher frequency than controls. The above courtship defects persisted when Fem-1 males courted control females, but no phenotypes were observed when control males courted Fem-1 females. These results indicate that Drosophila Fem-1 may interact with other genes involved in courtship and sex determination. Fem-1 mutants also suppressed wing and body growth, consistent with the actions of a homologue in mice. Additional analyses of these Fem-1 alleles will help address the nature of these mutations, deepen our molecular understanding of courtship, and contribute to the evolutionary relationships among this highly conserved gene family.

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 The amino acid sequence of cytochrome c from Nigella damascena L. (love-in-a-mist)

1973 ◽  
Vol 133 (2) ◽  
pp. 251-254 ◽  
Author(s):  
R. H. Brown ◽  
D. Boulter
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Science And Technology ◽  
The Other ◽  
Carboxypeptidase A ◽  
Cytochromes C ◽  
Lending Library ◽  
Nigella Damascena

The amino acid sequence of cytochrome c from Nigella damascena L. was determined on 0.2μmol of protein. Peptides from a single chymotryptic digest were analysed by the dansyl–Edman procedure. These peptides were ordered by reference to the sequences of other plant cytochromes c, assuming that the Nigella cytochrome is homologous with the other cytochromes. Many of the Nigella peptides were one or two residues short when compared with the corresponding chymotryptic peptides from other plant cytochromes c. These residues are assumed to have been removed by an endogenous carboxypeptidase, and the identification and placing of these residues is entirely based on homology. These residues are numbered 3, 18, 42, 43, 44, 54, 67, 72, 73, 82 and 105. A number of other positions are almost entirely placed by homology. These are positions which could not be placed definitely by dansyl–Edman analysis or by dansylation after digestion with carboxypeptidase A, and are numbered 14, 15, 16, 39, 40, 85, 86, 87 and 88. Except for residue 15, all residues based entirely, or nearly so, on homology have been previously found invariant in sequences of plant cytochromes c. Experimental details are given in a supplementary paper that has been deposited as Supplementary Publication SUP 50017, at the National Lending Library for Science and Technology, Boston Spa, Yorks. LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1973) 131, 5.

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