The S-adenosyl-l-homocysteine hydrolase of Drosophila melanogaster : identification, deduced amino acid sequence and cytological localization of the structural gene

1997 ◽  
Vol 253 (4) ◽  
pp. 492-498 ◽  
Author(s):  
C. Caggese ◽  
G. Ragone ◽  
P. Barsanti ◽  
R. Moschetti ◽  
A. Messina ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Structural Gene ◽  
Cytological Localization

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 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.

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.

scholarly journals Sequence of the Structural Gene for Xanthine Dehydrogenase (rosy Locus) in Drosophila melanogaster

Genetics ◽  
1987 ◽  
Vol 116 (1) ◽  
pp. 67-73
Author(s):  
Tim P Keith ◽  
Margaret A Riley ◽  
Martin Kreitman ◽  
R C Lewontin ◽  
Daniel Curtis ◽  
...  
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Drosophila Melanogaster ◽  
Amino Acid ◽  
Nucleotide Sequence ◽  
Structural Gene ◽  
Xanthine Dehydrogenase ◽  
Open Reading Frame ◽  
Reading Frame ◽  
Eco Ri

ABSTRACT We determined the nucleotide sequence of a 4.6-kb Eco RI fragment containing 70% of the rosy locus. In combination with information on the 5′ sequence, the gene has been sequenced in entirety. rosy cDNAs have been isolated and intron/exon boundaries have been determined. We find an open reading frame which spans four exons and would encode a protein of 1335 amino acids. The molecular weight of the encoded protein (xanthine dehydrogenase), based on the amino acid translation, is 146,898 daltons which agrees well with earlier biophysical estimates. Characteristics of the protein are discussed.

scholarly journals Characterization of a Novel PepF-Like Oligopeptidase Secreted by Bacillus amyloliquefaciens 23-7A

2006 ◽  
Vol 72 (1) ◽  
pp. 968-971 ◽  
Author(s):  
Shiou-Huei Chao ◽  
Tzu-Hao Cheng ◽  
Chin-Ying Shaw ◽  
Meng-Hwan Lee ◽  
Yuan-Hsun Hsu ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Structural Gene ◽  
Bacillus Amyloliquefaciens ◽  
Enzymatic Activities ◽  
Secreted Protein

ABSTRACT An oligopeptidase from Bacillus amyloliquefaciens 23-7A was characterized along with its biochemical activities and structural gene. The protein's amino acid sequence and enzymatic activities were similar to those of other bacterial PepFs, which belong to metallopeptidase family M3. While most bacterial PepFs are cytoplasmic endopeptidases, the identified PepFBa oligopeptidase is a secreted protein and may facilitate the process of sporulation.

scholarly journals Mutations Affecting Expression of the rosy Locus in Drosophila melanogaster

Genetics ◽  
1987 ◽  
Vol 116 (1) ◽  
pp. 55-66
Author(s):  
Chong Sung Lee ◽  
Daniel Curtis ◽  
Margaret McCarron ◽  
Carol Love ◽  
Mark Gray ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Xanthine Dehydrogenase ◽  
Control Element ◽  
Regulatory Change ◽  
Cdna Clones ◽  
Cdna Sequences ◽  
Regulatory Mutations ◽  
New Mutations

ABSTRACT The rosy locus in Drosophila melanogaster codes for the enzyme xanthine dehydrogenase (XDH). Previous studies defined a "control element" near the 5′ end of the gene, where variant sites affected the amount of rosy mRNA and protein produced. We have determined the DNA sequence of this region from both genomic and cDNA clones, and from the ry  +10 underproducer strain. This variant strain had many sequence differences, so that the site of the regulatory change could not be fixed. A mutagenesis was also undertaken to isolate new regulatory mutations. We induced 376 new mutations with 1-ethyl-1-nitrosourea (ENU) and screened them to isolate those that reduced the amount of XDH protein produced, but did not change the properties of the enzyme. Genetic mapping was used to find mutations located near the 5′ end of the gene. DNA from each of seven mutants was cloned and sequenced through the 5′ region. Mutant base changes were identified in all seven; they appear to affect splicing and translation of the rosy mRNA. In a related study (T. P. Keith et al. 1987), the genomic and cDNA sequences are extended through the 3′ end of the gene; the combined sequences define the processing pattern of the rosy transcript and predict the amino acid sequence of XDH.

Ribosomal protein S14 is encoded by a pair of highly conserved, adjacent genes on the X chromosome of Drosophila melanogaster

1988 ◽  
Vol 8 (10) ◽  
pp. 4314-4321
Author(s):  
S J Brown ◽  
D D Rhoads ◽  
M J Stewart ◽  
B Van Slyke ◽  
I T Chen ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Drosophila Melanogaster ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Ribosomal Protein ◽  
X Chromosome ◽  
Duplicated Genes ◽  
Ribosomal Protein Genes ◽  
Yeast Saccharomyces Cerevisiae ◽  
Genes Encoding

We describe a Drosophila DNA clone of tandemly duplicated genes encoding an amino acid sequence nearly identical to human ribosomal protein S14 and yeast rp59. Despite their remarkably similar exons, the locations and sizes of introns differ radically among the Drosophila, human, and yeast (Saccharomyces cerevisiae) ribosomal protein genes. Transcripts of both Drosophila RPS14 genes were detected in embryonic and adult tissues and are the same length as mammalian S14 message. Drosophila RPS14 was mapped to region 7C5-9 on the X chromosome. This interval also encodes a previously characterized Minute locus, M(1)7C.

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