Pupal and larval cuticle proteins of Drosophila melanogaster

Biochemistry ◽  
1984 ◽  
Vol 23 (24) ◽  
pp. 5767-5774 ◽  
Author(s):  
Donald J. Silvert ◽  
John Doctor ◽  
Luis Quesada ◽  
James W. Fristrom
Keyword(s):  
Drosophila Melanogaster ◽  
Larval Cuticle ◽  
Cuticle Proteins

scholarly journals A Cluster of Cuticle Protein Genes of Drosophila melanogaster at 65A: Sequence, Structure and Evolution

Genetics ◽  
1997 ◽  
Vol 147 (3) ◽  
pp. 1213-1224
Author(s):  
Jean-Philippe Charles ◽  
Carol Chihara ◽  
Shamim Nejad ◽  
Lynn M Riddiford
Keyword(s):  
Drosophila Melanogaster ◽  
Genomic Dna ◽  
Multiple Copy ◽  
Sequence Structure ◽  
Coding Regions ◽  
The Third ◽  
Genetic Complexity ◽  
Genes Encoding ◽  
Cuticle Protein ◽  
Cuticle Proteins

A 36-kb genomic DNA segment of the Drosophila melanogaster genome containing 12 clustered cuticle genes has been mapped and partially sequenced. The cluster maps at 65A 5-6 on the left arm of the third chromosome, in agreement with the previously determined location of a putative cluster encompassing the genes for the third instar larval cuticle proteins LCP5, LCP6 and LCP8. This cluster is the largest cuticle gene cluster discovered to date and shows a number of surprising features that explain in part the genetic complexity of the LCP5, LCP6 and LCP8 loci. The genes encoding LCP5 and LCP8 are multiple copy genes and the presence of extensive similarity in their coding regions gives the first evidence for gene conversion in cuticle genes. In addition, five genes in the cluster are intronless. Four of these five have arisen by retroposition. The other genes in the cluster have a single intron located at an unusual location for insect cuticle genes.

The origin of pattern duplications in segment polarity mutants of Drosophila melanogaster

Development ◽  
1985 ◽  
Vol 87 (1) ◽  
pp. 129-135
Author(s):  
Alfonso Martinez-Arias ◽  
Philip W. Ingham
Keyword(s):  
Drosophila Melanogaster ◽  
Bithorax Complex ◽  
Anterior Compartment ◽  
Larval Cuticle ◽  
Segment Polarity ◽  
Reversed Polarity ◽  
Segmental Identity

Mutations of the segment polarity group in Drosophila melanogaster produce additional denticles with reversed polarity in every segment of the larval cuticle. We have investigated the effect of mutations in different elements of the bithorax complex on the segmental identity of these additional pattern elements. Our results suggest that they are derived, primarily, from the anterior compartment of each segment.

The cuticle proteins of Drosophila melanogaster: Stage specificity

1982 ◽  
Vol 89 (2) ◽  
pp. 379-388 ◽  
Author(s):  
Carol J. Chihara ◽  
Donald J. Silvert ◽  
James W. Fristrom
Keyword(s):  
Drosophila Melanogaster ◽  
Stage Specificity ◽  
Cuticle Proteins

Purification and cDNA cloning of evolutionally conserved larval cuticle proteins of the silkworm, Bombyx mori

1997 ◽  
Vol 27 (8-9) ◽  
pp. 701-709 ◽  
Author(s):  
Hiroshi Nakato ◽  
Mariko Takekoshi ◽  
Toru Togawa ◽  
Susumu Izumi ◽  
Shiro Tomino
Keyword(s):  
Bombyx Mori ◽  
Cdna Cloning ◽  
Larval Cuticle ◽  
Cuticle Proteins ◽  
Silkworm Bombyx Mori

Analysis of DNA structural patterns and sequence organization at the larval cuticle locus in Drosophila melanogaster

1983 ◽  
Vol 3 (10) ◽  
pp. 1724-1729
Author(s):  
J C Eissenberg ◽  
S C Elgin
Keyword(s):  
Drosophila Melanogaster ◽  
Sequence Data ◽  
Micrococcal Nuclease ◽  
Dominant Factor ◽  
Base Pairs ◽  
Element Analysis ◽  
Larval Cuticle ◽  
Sequence Organization ◽  
General Base ◽  
Dna Organization

We examined the pattern of DNA organization at the larval cuticle gene complex 44D of Drosophila melanogaster, using micrococcal nuclease and the 1,10-phenanthroline-cuprous complex. The initial cleavage patterns obtained with both reagents exhibited "gaps" at the positions of each of the genes examined, as well as at a pseudogene sequence contained within the complex. An additional gap for which no gene exists was observed for both patterns. The cleavage pattern obtained with micrococcal nuclease was unaltered, at a level of resolution of +/- 50 base pairs, in a mutant containing a transposable element. Analysis of the sequence data from this 5.5-kilobase gene cluster indicated that the sequence per se, and not the general base composition, is a dominant factor in determining the patterns observed.

Larval cuticle proteins of Lucilia cuprina

1987 ◽  
Vol 17 (4) ◽  
pp. 625-633 ◽  
Author(s):  
P.J. Skelly ◽  
A.J. Howells
Keyword(s):  
Lucilia Cuprina ◽  
Larval Cuticle ◽  
Cuticle Proteins

scholarly journals mRNA and Small RNA-seq Reveal Insights into Immune Regulation in Apis cerana after Chinese Sacbrood Virus Infection

2020 ◽  
Author(s):  
Yanchun Deng ◽  
Hongxia Zhao ◽  
Shuo Shen ◽  
Sa Yang ◽  
Dahe Yang ◽  
...  
Keyword(s):  
Immune Response ◽  
Fatty Acid ◽  
Target Genes ◽  
Fatty Acid Biosynthesis ◽  
Apis Cerana ◽  
Larval Cuticle ◽  
Go Annotation ◽  
Kegg Analysis ◽  
Sacbrood Virus ◽  
Cuticle Proteins

Chinese sacbrood virus (CSBV) is a serious threat to eastern honeybees (Apis cerana), especially larvae. However, the pathological mechanism of this deadly disease is remains unclear. Here, we employed an mRNA-seq and sRNA-seq approach in healthy and CSBV-infected 3rd Apis cerana larval. Gene ontology (GO) and KEGG analysis of 203 differentially expressed genes showed that CSBV infection affected host development by up-regulating the expression of larval cuticle proteins, such as larval cuticle proteins A1A and A3A, resulting in elevated susceptibility to CSBV. In addition, viral infection not only affected the expression of serine protease related to the melanization pathway and but also altered fatty acid metabolism and biosynthesis, thus progressed to disturb host immune response. Interestingly, GO annotation and KEGG analysis on target genes of CSBV-specific siRNA (vsiRNAs) showed that serine/threonine kinase activity and serine-type endopeptidas as well as fatty acid biosynthesis were significantly enriched (P < 0.05). Among these vsiRNAs, vsiRNA-1441 with relatively high expression targeted extracellular serine/threonine protein kinase. This study provides new evidence that CSBV attacks a distinct immune response pathway and mediates the expression of cuticle protein to gain the more chance of proliferation.

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