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<h1 id="firstHeading" class="firstHeading mw-first-heading"><span class="mw-page-title-main">Primase</span></h1>
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<div id="mw-content-text" class="mw-body-content mw-content-ltr" lang="de" dir="ltr"><div class="mw-content-ltr mw-parser-output" lang="de" dir="ltr"><table class="wikitable hintergrundfarbe-basis infobox float-right" id="Vorlage_Infobox_Protein_dnaG_(E._coli)" style="font-size:90%; margin-top:0; width:350px;" summary="Infobox Protein">
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<th colspan="3" style="background:#90EE90; color:#202122;">dnaG (<i>E. coli</i>)
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<td colspan="3" class="hintergrundfarbe1" style="text-align:center; font-size:smaller; font-weight:bold;">dnaG Bänder-/Oberflächenmodell nach <a href="Protein_Data_Bank" title="Protein Data Bank">PDB</a> <a rel="nofollow" class="external text" href="https://www.rcsb.org/structure/3B39">3B39</a>
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<td><a href="Molare_Masse" title="Molare Masse">Masse</a>/Länge <a href="Prim%C3%A4rstruktur" title="Primärstruktur">Primärstruktur</a>
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<td colspan="2" style="text-align:center;">581 Aminosäuren
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<td><a href="Sekund%C3%A4rstruktur" title="Sekundärstruktur">Sekundär-</a> bis <a href="Quart%C3%A4rstruktur" title="Quartärstruktur">Quartärstruktur</a>
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<td colspan="2" style="text-align:center;">Monomer
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<td><a href="Koenzym" class="mw-redirect" title="Koenzym">Kofaktor</a>
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<td colspan="2" style="text-align:center;">Zn<sup>2+</sup>
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<th colspan="3" style="background:#90EE90; color:#202122;">Bezeichner
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<td>Externe IDs
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<ul><li><a href="UniProt" title="UniProt">UniProt</a> <a rel="nofollow" class="external text" href="https://www.uniprot.org/uniprotkb/P0ABS5">P0ABS5</a></li>
<li><a href="CAS-Nummer" title="CAS-Nummer">CAS-Nummer</a>: <span title="Untervorlage eingebunden: CASRN"></span><a rel="nofollow" class="external text" href="https://commonchemistry.cas.org/detail?cas_rn=9014-24-8">9014-24-8</a><span class="editoronly" style="display:none;"></span></li></ul>
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<th colspan="3" style="background:#90EE90; color:#202122;">Enzymklassifikation
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<td><a href="EC-Nummer" title="EC-Nummer">EC, Kategorie</a>
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<td colspan="2" class="" style="text-align:center;"><a rel="nofollow" class="external text" href="https://www.brenda-enzymes.org/enzyme.php?ecno=2.7.7.-">2.7.7.-</a>, <a href="Nukleotidyltransferase" title="Nukleotidyltransferase">Nukleotidyltransferase</a>
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<td>Reaktionsart
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<td colspan="2" style="text-align:center;">Nukleotid-<a href="Additionsreaktion" title="Additionsreaktion">Addition</a>
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<td>Substrat
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<td colspan="2" style="text-align:center;">Nucleosidtriphosphat + RNA<sub>n</sub>
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<td>Produkte
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<td colspan="2" style="text-align:center;">Diphosphat + RNA<sub>n+1</sub>
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<th colspan="3" style="background:#90EE90; color:#202122;">Vorkommen
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<td style="background:#C3FDB8; color:#202122;">Homologie-Familie
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<td colspan="2" style="text-align:center;"><a rel="nofollow" class="external text" href="http://hogenom.univ-lyon1.fr/query_sequence?seq=P0ABS5">DNA Primase</a>
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<td style="background:#C3FDB8; color:#202122;">Übergeordnetes <a href="Taxon" title="Taxon">Taxon</a>
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<td colspan="2" style="text-align:center;"><a href="Bakterien" title="Bakterien">Bakterien</a>
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</p><p><b>Primase</b> ist der Name für eine <a href="RNA-Polymerase" class="mw-redirect" title="RNA-Polymerase">RNA-Polymerase</a>, also ein <a href="Enzym" title="Enzym">Enzym</a>. Primasen sind Bestandteile von <a href="Primosom" title="Primosom">Primosomen</a> (Ssb-Protein+Helikase+Primase), die bei der Initiation der <a href="DNA-Replikation" class="mw-redirect" title="DNA-Replikation">Verdopplung des Erbmaterials</a> eine Rolle spielen.
</p><p>Dabei erzeugt die Primase ein kurzes <a href="RNA" class="mw-redirect" title="RNA">RNA</a>-Startmolekül, den <a href="Primer" title="Primer">Primer</a>. Dieser Primer lagert sich an die komplementäre Sequenz auf der <a href="Desoxyribonukleins%C3%A4ure" title="Desoxyribonukleinsäure">DNA</a> an. Das entstehende Stückchen Doppelstrang wird von der <a href="DNA-Polymerase" class="mw-redirect" title="DNA-Polymerase">DNA-Polymerase</a> als Ansatzstelle für die Verlängerung (<a href="Elongation_(Transkription)" title="Elongation (Transkription)">Elongation</a>) des DNA-Stranges genutzt.
</p><p>Die Primase der <a href="Prokaryoten" title="Prokaryoten">Prokaryoten</a> ist das DnaG-Protein. In <a href="Eukaryoten" title="Eukaryoten">Eukaryoten</a> besteht die Primase aus zwei Untereinheiten, die als Teil der DNA-Polymerase α das Priming erledigen.
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<div class="mw-heading mw-heading2"><h2 id="Literatur">Literatur</h2></div>
<ul><li>Bocquier, Arnaud A. (2001). "Archaeal primase". Current Biology 11 (6): 452–456.</li>
<li>Griep, Mark A. (1995). "Primase Structure and Function". Indian Journal of Biochemistry & Biophysics 32 (4): 171–8. <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/8655184?dopt=Abstract">PMID 8655184</a>.</li>
<li>Keck, James L., and Daniel D. Roche, A. Simon Lynch, James M. Berger. (2000). "Structure of the RNA Polymerase Domain of E. coli Primase". Science 282 (5462): 2482–6. <a href="Digital_Object_Identifier" title="Digital Object Identifier">doi</a>:<span class="uri-handle" style="white-space:nowrap"><a rel="nofollow" class="external text" href="https://doi.org/10.1126/science.287.5462.2482">10.1126/science.287.5462.2482</a></span>. <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/10741967?dopt=Abstract">PMID 10741967</a>.</li>
<li>Lee, Jong-Bong, and Richard K. Hite, Samir M. Hamdan et al. (2006). "DNA primase acts as a molecular brake in DNA replication". Nature 439 (7076): 621–624. <a href="Digital_Object_Identifier" title="Digital Object Identifier">doi</a>:<span class="uri-handle" style="white-space:nowrap"><a rel="nofollow" class="external text" href="https://doi.org/10.1038/nature04317">10.1038/nature04317</a></span>. <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/16452983?dopt=Abstract">PMID 16452983</a>.</li>
<li>Cavanaugh, Nisha A., and Robert D. Kuchta (2009). "Initiation of New DNA Strands by the Herpes Simplex Virus-1 Primase-Helicase Complex and Either Herpes DNA Polymerase or Human DNA Polymerase alpha". J. Biol. Chem. 284 (3): 1523–1532. <a href="Digital_Object_Identifier" title="Digital Object Identifier">doi</a>:<span class="uri-handle" style="white-space:nowrap"><a rel="nofollow" class="external text" href="https://doi.org/10.1074/jbc.M805476200">10.1074/jbc.M805476200</a></span>. <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2615532/">PMC 2615532</a> (freier Volltext). <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/19028696?dopt=Abstract">PMID 19028696</a>.</li></ul></div><!--htdig_noindex--><div><div class="zim-footer">
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