The actin genes of drosophila: Protein coding regions are highly conserved but intron positions are not

Fyrberg, Eric; Bond, Beverley J.; Hershey, Neil D.; Mixter, Katharine S.; Davidson, Norman

doi:10.1016/0092-8674(81)90506-7

Cited by 321 publications

(160 citation statements)

References 25 publications

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“…The problem derives from the following considerations. First, the presence of a cysteine residue at amino acid 1 (referred to as "Cys+") is unique to protostome and deuterostome actin genes (2,6,7,29), whereas all actin genes in more primitive organisms lack this residue (called "Cys-") (5, 8, 16). Second, the ubiquitous occurrence of both Cys+ and a mechanism to remove the aminoterminal cysteine in both protostomes and deuterostomes is too coincidental to be explained by convergent evolution.…”

Section: Discussionmentioning

confidence: 99%

“…Note the presence of a cysteine codon immediately after the initiator methionine codon in a-actin (boxed) but not in or y-actin mRNA. mRNA contains the consensus sequence CAA Pu AUG found at the initiation site of five of the six Drosophila actin genes (7).…”

Section: Figmentioning

confidence: 99%

“…However, in all published reports to date regarding protostome and deuterostome actin genes this methionine codon is always followed by a cysteine codon. This is true of all six actin genes in Drosophila melanogaster (7). It is also of interest that although all these Drosophila genes encode cytoplasmic-like actin proteins, some are expressed in muscle.…”

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confidence: 99%

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Isolation and characterization of full-length cDNA clones for human alpha-, beta-, and gamma-actin mRNAs: skeletal but not cytoplasmic actins have an amino-terminal cysteine that is subsequently removed.

Gunning¹,

Ponte²,

Okayama³

et al. 1983

Mol. Cell. Biol.

965

348

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cDNA clones encoding three classes of human actins have been isolated and characterized. The first two classes (y and ,B, cytoplasmic actins) were obtained from a cDNA library constructed from simian virus 40-transformed human fibroblast mRNA, and the third class (a, muscle actin) was obtained from a cDNA library constructed from adult human muscle mRNA. A new approach was developed to enrich for full-length cDNAs. The human fibroblast cDNA plasmid library was linearized with restriction enzymes that did not cut the inserts of interest; it was then size-fractionated on gels, and the chimeric molecules of optimal length were selected for retransformation of bacteria. When the resulting clones were screened for actin-coding sequences it was found that some fulllength cDNAs were enriched as much as 50-to 100-fold relative to the original frequency of full-length clones in the total library. Two types of clones were distinguished. One of these clones encodes y actin and contains 100 base pairs of 5' untranslated region, the entire protein coding region, and the 3' untranslated region. The second class encodes 1 actin, and the longest such clone contains 45 base pairs of 5' untranslated region plus the remainder of the mRNA extending to the polyadenylic acid tail. A third class, obtained from the human muscle cDNA library, encodes a actin and contains 100 base pairs of 5' untranslated region, the entire coding region, and the 3' untranslated region. Analysis of the DNA sequences of the 5' end of the clones demonstrated that although 13-and y-actin

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Section: Discussionmentioning

confidence: 99%

Section: Figmentioning

confidence: 99%

See 1 more Smart Citation

Isolation and characterization of full-length cDNA clones for human alpha-, beta-, and gamma-actin mRNAs: skeletal but not cytoplasmic actins have an amino-terminal cysteine that is subsequently removed.

Gunning¹,

Ponte²,

Okayama³

et al. 1983

Mol. Cell. Biol.

965

348

View full text Add to dashboard Cite

show abstract

“…The open reading frame regions of the cDNAs encoding cecropin A1 (33), drosomycin (34), and attacin (35) were amplified by PCR, and each amplified PCR product was used as probe. The ␤-actin cDNA was used as an internal standard probe (36). For inhibition experiment by anti-DGNBP-1 antiserum, cells were pretreated with either DGNBP-1 antiserum or pre-immune serum at the final concentration of 1% for 1 h at room temperature before stimulation.…”

Section: Methodsmentioning

confidence: 99%

Gram-negative Bacteria-binding Protein, a Pattern Recognition Receptor for Lipopolysaccharide and β-1,3-Glucan That Mediates the Signaling for the Induction of Innate Immune Genes in Drosophila melanogaster Cells

Kim

Ryu

Han

et al. 2000

Journal of Biological Chemistry

272

185

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“…# . The sequences of the primers were : DMKP, sense, 5h-CCCGCGTCAATGGAGTT-TATTG-3h, and antisense, 5h-TTAACTGTTGTATGAATCC-CGC-3h ; β-actin, sense, 5h-GATCACCATTGGCAACGA-3h, and antisense, 5h-TCTTGATCTTGATGGTCG-3h [33]. The optimal number of cycles for RT-PCR was determined as described previously [34].…”

Section: Construction Of Plasmidsmentioning

confidence: 99%

Inhibition of mitogen-activated protein kinase by a Drosophila dual-specific phosphatase

Lee

Kim

et al. 2000

Biochemical Journal

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The Drosophila extracellular signal-regulated kinase (DERK) mitogen-activated protein kinase (MAPK) is involved in the regulation of multiple differentiation and developmental processes. Tight control of MAPK activity is critical for normal cell behaviour. We identified a novel Drosophila MAPK phosphatase (DMKP) cDNA from the expressed-sequence-tag database and characterized it. Analysis of the nucleotide sequence revealed an open reading frame encoding the 203-amino acid protein, with a calculated molecular mass of 23kDa, which has a high amino acid sequence similarity with ‘VH1-like’dual-specific phosphatases at the broad region near the catalytic sites. The expression of DMKP mRNA occurs from the late larval stages to adulthood in Drosophila development. The recombinant DMKP protein produced in yeast retained its phosphatase activity. When expressed in Schneider cells, DMKP dose-dependently inhibited DERK and Drosophila c-Jun N-terminal kinase activities with high selectivity towards DERK. However, DMKP did not have any affect on Drosophila p38 activity. When DMKP was expressed in yeast, it down-regulated the fus1-lacZ trans-reporter gene of the pheromone MAPK pathway without any significant effect on the high-osmolarity-glycerol-response pathway.

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The actin genes of drosophila: Protein coding regions are highly conserved but intron positions are not

Cited by 321 publications

References 25 publications

Isolation and characterization of full-length cDNA clones for human alpha-, beta-, and gamma-actin mRNAs: skeletal but not cytoplasmic actins have an amino-terminal cysteine that is subsequently removed.

Isolation and characterization of full-length cDNA clones for human alpha-, beta-, and gamma-actin mRNAs: skeletal but not cytoplasmic actins have an amino-terminal cysteine that is subsequently removed.

Gram-negative Bacteria-binding Protein, a Pattern Recognition Receptor for Lipopolysaccharide and β-1,3-Glucan That Mediates the Signaling for the Induction of Innate Immune Genes in Drosophila melanogaster Cells

Inhibition of mitogen-activated protein kinase by a Drosophila dual-specific phosphatase

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