Wang Zhibo, Cotney Justin, Shadel Gerald S
Department of Pathology, Yale University School of Medicine, New Haven, Connecticut 06520-8023, USA.
J Biol Chem. 2007 Apr 27;282(17):12610-8. doi: 10.1074/jbc.M700461200. Epub 2007 Mar 2.
The core human mitochondrial transcription machinery comprises a single subunit bacteriophage-related RNA polymerase, POLRMT, the high mobility group box DNA-binding protein h-mtTFA/TFAM, and two transcriptional co-activator proteins, h-mtTFB1 and h-mtTFB2 that also have rRNA methyltransferase activity. Recapitulation of specific initiation of transcription in vitro can be achieved by a complex of POL-RMT, h-mtTFA, and either h-mtTFB1 or h-mtTFB2. However, the nature of mitochondrial transcription complexes in vivo and the potential involvement of additional proteins in the transcription process in human mitochondria have not been extensively investigated. In Saccharomyces cerevisiae, transcription and translation are physically coupled via the formation of a multiprotein complex nucleated by the binding of Nam1p to the amino-terminal domain of mtRNA polymerase (Rpo41p). This model system paradigm led us to search for proteins that interact with POLRMT to regulate mitochondrial gene expression in humans. Using an affinity capture strategy to identify POL-RMT-binding proteins, we identified mitochondrial ribosomal protein L7/L12 (MRPL12) as a protein in HeLa mitochondrial extracts that interacts specifically with POLRMT in vitro. Purified recombinant MRPL12 binds to POLRMT and stimulates mitochondrial transcription activity in vitro, demonstrating that this interaction is both direct and functional. Finally, from HeLa cells that overexpress FLAG epitope-tagged MRPL12, increased steady-state levels of mtDNA-encoded transcripts are observed and MRPL12-POLRMT complexes can be co-immunoprecipitated, providing strong evidence that this interaction enhances mitochondrial transcription or RNA stability in vivo. We speculate that the MRPL12 interaction with POLRMT is likely part of a novel regulatory mechanism that coordinates mitochondrial transcription with translation and/or ribosome biogenesis during human mitochondrial gene expression.
人类线粒体转录核心机制由单个亚基的噬菌体相关RNA聚合酶POLRMT、高迁移率族框DNA结合蛋白h-mtTFA/TFAM以及两种也具有rRNA甲基转移酶活性的转录共激活蛋白h-mtTFB1和h-mtTFB2组成。体外转录特异性起始的重现可通过POL-RMT、h-mtTFA以及h-mtTFB1或h-mtTFB2的复合物来实现。然而,体内线粒体转录复合物的性质以及其他蛋白质在人类线粒体转录过程中的潜在作用尚未得到广泛研究。在酿酒酵母中,转录和翻译通过由Nam1p与线粒体RNA聚合酶(Rpo41p)的氨基末端结构域结合所形成的多蛋白复合物在物理上偶联。这种模型系统范例促使我们寻找与POLRMT相互作用以调节人类线粒体基因表达的蛋白质。利用亲和捕获策略鉴定POL-RMT结合蛋白,我们在HeLa线粒体提取物中鉴定出线粒体核糖体蛋白L7/L12(MRPL12)为一种在体外与POLRMT特异性相互作用的蛋白质。纯化的重组MRPL12与POLRMT结合并在体外刺激线粒体转录活性,表明这种相互作用既是直接的也是功能性的。最后,在过表达FLAG表位标签的MRPL12的HeLa细胞中,观察到mtDNA编码转录本稳态水平升高,并且MRPL12-POLRMT复合物可被共免疫沉淀,这提供了强有力的证据表明这种相互作用在体内增强了线粒体转录或RNA稳定性。我们推测MRPL12与POLRMT的相互作用可能是一种新的调节机制的一部分,该机制在人类线粒体基因表达过程中协调线粒体转录与翻译和/或核糖体生物发生。