Amylase synthesis as a simple model system for translation and hybrid arresst in Xenopus oocytes
Identifieur interne : 000507 ( Istex/Curation ); précédent : 000506; suivant : 000508Amylase synthesis as a simple model system for translation and hybrid arresst in Xenopus oocytes
Auteurs : Mark S. Urnes [États-Unis] ; Dana Carroll [États-Unis]Source :
- Gene [ 0378-1119 ] ; 1990.
English descriptors
- Teeft :
- Amylase, Antisense, Antisense oligo, Antisense oligos, Assay, Blue starch, Cdna, Coding sequence, Error bars, Expression system, External medium, External samples, Incubation medium, Individual oocytes, Internal control, Internal pool, Kidney mrna, Methods enzymol, Mrna, Nucleic acids, Oligo, Oligos, Oocyte, Oocyte cytoplasm, Oocyte homogenates, Oocyte translation, Other mrnas, Pancreatic gene, Room temperature, Salt lake city, Secretory capacity, Secretory machinery, Several experiments, Signal sequence, Stable hybrids, Standard deviations, Synthetic mrna, Transcription, Transcription vector, Translational, Uninjected oocytes, Utah school, Western blots, Xenopus, Xenopus oocytes.
Abstract
Abstract: A human α-amylase-encoding cDNA has been cloned in a transcription vector. When messenger RNA (mRNA) made in vitro from this construct was injected into Xenopus oocytes, amylase (AMY) activity was detected both in oocyte homogenates and in the incubation medium, indicating that the oocyte machinery correctly translated and processed the protein. Because AMY activity is easy to detect with a blue-starch assay, this expression system was used to determine the parameters of antisense oligodeoxyribunucleotide (oligo) inhibition of translation in the oocytes. Unique oligos complementary to the AMY mRNA sequence were effective in arresting translation, at approximately stoichiometric levels. Mixed oligos also inhibited translation, at levels that suggest that some mismatches may be tolerated in the formation of DNA-RNA hybrids. The AMY system provides a convenient probe of oocyte protein synthesis and processing machinery and can serve as a control substrate in investigations of other mRNAs.
Url:
DOI: 10.1016/0378-1119(90)90370-7
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Urnes</name><affiliation wicri:level="2"><mods:affiliation>Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, UT 84132 U.S.A.</mods:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Utah</region></placeName><wicri:cityArea>Department of Biochemistry, University of Utah School of Medicine, Salt Lake City</wicri:cityArea></affiliation></author><author><name sortKey="Carroll, Dana" sort="Carroll, Dana" uniqKey="Carroll D" first="Dana" last="Carroll">Dana Carroll</name><affiliation wicri:level="2"><mods:affiliation>Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, UT 84132 U.S.A.</mods:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Utah</region></placeName><wicri:cityArea>Department of Biochemistry, University of Utah School of Medicine, Salt Lake City</wicri:cityArea></affiliation></author></analytic><monogr></monogr><series><title level="j">Gene</title><title level="j" type="abbrev">GENE</title><idno type="ISSN">0378-1119</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1990">1990</date><biblScope unit="volume">95</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="267">267</biblScope><biblScope unit="page" to="274">274</biblScope></imprint><idno type="ISSN">0378-1119</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0378-1119</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Amylase</term><term>Antisense</term><term>Antisense oligo</term><term>Antisense oligos</term><term>Assay</term><term>Blue starch</term><term>Cdna</term><term>Coding sequence</term><term>Error bars</term><term>Expression system</term><term>External medium</term><term>External samples</term><term>Incubation medium</term><term>Individual oocytes</term><term>Internal control</term><term>Internal pool</term><term>Kidney mrna</term><term>Methods enzymol</term><term>Mrna</term><term>Nucleic acids</term><term>Oligo</term><term>Oligos</term><term>Oocyte</term><term>Oocyte cytoplasm</term><term>Oocyte homogenates</term><term>Oocyte translation</term><term>Other mrnas</term><term>Pancreatic gene</term><term>Room temperature</term><term>Salt lake city</term><term>Secretory capacity</term><term>Secretory machinery</term><term>Several experiments</term><term>Signal sequence</term><term>Stable hybrids</term><term>Standard deviations</term><term>Synthetic mrna</term><term>Transcription</term><term>Transcription vector</term><term>Translational</term><term>Uninjected oocytes</term><term>Utah school</term><term>Western blots</term><term>Xenopus</term><term>Xenopus oocytes</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: A human α-amylase-encoding cDNA has been cloned in a transcription vector. When messenger RNA (mRNA) made in vitro from this construct was injected into Xenopus oocytes, amylase (AMY) activity was detected both in oocyte homogenates and in the incubation medium, indicating that the oocyte machinery correctly translated and processed the protein. Because AMY activity is easy to detect with a blue-starch assay, this expression system was used to determine the parameters of antisense oligodeoxyribunucleotide (oligo) inhibition of translation in the oocytes. Unique oligos complementary to the AMY mRNA sequence were effective in arresting translation, at approximately stoichiometric levels. Mixed oligos also inhibited translation, at levels that suggest that some mismatches may be tolerated in the formation of DNA-RNA hybrids. The AMY system provides a convenient probe of oocyte protein synthesis and processing machinery and can serve as a control substrate in investigations of other mRNAs.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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