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. RNA synthesis by RNA polymerases occurs in three steps: initiation, elongation and termination. We have new crystals of different DNA promoter constructs bound to the T7 RNA polymerase to determine which features of the template and the enzyme that involved in promoter strength, fidelity of transcription and nucleotide selection. The biological relevance of this work would illustrate structural basis for promoter-dependent enzymatic activities. References 1. Cheetham GM, Steitz TA. Structure of a transcribing T7 RNA polymerase initiation complex. Science 286:2305. 1999 2. Cheetham GM, Jeruzalmi D, Steitz TA. Structural basis for initiation of transcription from an RNA polymerase-promoter complex. Nature 399:80. 1999 3. Yin YW, Steitz TA. Structural basis for the transition from initiation to elongation transcription in T7 RNA polymerase. Science 298: 1387. 2002 4. Yin YW, Steitz TA. Power stroke and ratchet translocation in T7 RNA polymerase Cell 116: 393. (2004) 5. Ikeda, RA, Chang LL, Warshamana GS. Selection and characterization of a mutant T7 RNA polymerase that recognizes an expanded range of T7 promoter-like sequences. Biochemistry 1993, 32:9115-24 6. Brieba, LG and Sousa, R. Roles of histadine 784 and tyrosine 639 in ribose discrimination by T7 RNA polymerase. Biochemistry 39:919. 2000
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