STRUCTURAL STUDIES OF THE CLASS I LIGASE RIBOZYME
STRUCTURAL STUDIES OF THE CLASS I LIGASE RIBOZYME
批准号:
7721216
负责人:
DAVID P BARTEL
金额:
$0.7万
依托单位:
依托单位国家:
美国
项目类别:
财政年份:
2008
资助国家:
美国
项目状态:
已结题
起止时间:
2008-05-15 至 2009-03-31
关键词:
BiogenesisCatalytic RNAClassComputer Retrieval of Information on Scientific Projects DatabaseDiphosphatesEnzymatic BiochemistryFundingGrantInstitutionLigaseNucleotidesOligonucleotidesPolymerasePrimer ExtensionProcessRNARNA-Directed RNA PolymeraseResearchResearch PersonnelResourcesSourceUnited States National Institutes of HealthVariantbasephosphodiestertripolyphosphate
中文摘要
这个子项目是许多利用
由NIH/NCRR资助的中心赠款提供的资源。子项目和
研究者(PI)可能从另一个NIH来源获得了主要资金,
因此可在其他CRISP条目中表示。所列机构为
研究中心,而研究中心不一定是研究者所在的机构。
从随机序列从头产生I类连接酶核酶。 这种催化性RNA加速小寡核苷酸的3 'OH对其自身的5'-末端三磷酸的攻击,产生3 '-5'磷酸二酯键和焦磷酸。我们已经产生了核酶的变体,其执行引物延伸以产生可以延伸任何模板-引物对的一般聚合酶核酶,通常最多14个核苷酸。 在RNA世界假说中,这种依赖RNA的RNA聚合酶活性可能是导致生命起源的过程的关键组成部分。 因此,I类连接酶核酶是一个非常有吸引力的目标,晶体学分析,以了解这种原始酶学的结构基础。
英文摘要
This subproject is one of many research subprojects utilizing the
resources provided by a Center grant funded by NIH/NCRR. The subproject and
investigator (PI) may have received primary funding from another NIH source,
and thus could be represented in other CRISP entries. The institution listed is
for the Center, which is not necessarily the institution for the investigator.
The class I ligase ribozyme was generated de novo from random sequences. This catalytic RNA accelerates the attack of a small oligonucleotide's 3'OH on its own 5'-terminal triphosphate, yielding a 3'-5' phosphodiester linkage and pyrophosphate. We have generated variants of the ribozyme which are perform primer extension to produced a general polymerase ribozyme which can extend any template-primer pair, often by up to 14 nucleotides. In the RNA world hypothesis, this type of RNA-dependent RNA-polymerase activity would have been a critical component of the processes that led to the origins of life. Thus the class I ligase ribozyme is an extremely attractive target for crystallographic analysis in order to understand the structural basis for this primordial enzymology.
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