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Rigor, reproducibility, and transparency (RR&T) are essential components of all scientific pursuits. Shared research resources, also known as core facilities, are on the frontlines of ensuring robust RR&T practices. The Association of Biomolecular Resource Facilities Committee on Core Rigor and Reproducibility conducted a follow-up survey 4 years after the initial 2017 survey to determine if core facilities have seen a positive impact of new RR&T initiatives (including guidance from the National Institutes of Health, new scientific journal requirements on transparency and data provenance, and educational tools from professional organizations). While there were fewer participants in the most recent survey, the respondents’ opinions on the role of core facilities and level of best practices adoption remained the same. Overall, the respondents agreed that procedures should be implemented by core facilities to ensure scientific RR&T. They also indicated that there is a strong correlation between institutions that emphasize RR&T and core customers using this expertise in grant applications and publications. The survey also assessed the impact of the COVID-19 pandemic on core operations and RR&T. The answers to these pandemic-related questions revealed that many of the strategies aimed at increasing efficiencies are also best practices related to RR&T, including the development of standard operating procedures, supply chain management, and cross training. Given the consistent and compelling awareness of the importance of RR&T expressed by core directors in 2017 and 2021 contrasted with the lack of apparent improvements over this time period, the authors recommend an adoption of RR&T statements by all core laboratories. Adhering to the RR&T guidelines will result in more efficient training, better compliance, and improved experimental approaches empowering cores to become “rigor champions.”

Using fractionated Xenopus transcription factors we have identified and characterized a unique protein-DNA complex formed between TFIIIA, TFIIIC and a 5S RNA gene. The formation of this complex was blocked by specific competitor DNAs and by the inactivation of TFIIIC using two different methods. In addition, TFIIIC activity was retained when the complexes were affinity purified using a reversibly immobilized DNA template. The TFIII(A+C)-5S RNA gene complex has a distinct electrophoretic mobility on band-shift gels and a unique DNase I footprint. The characteristic feature of the DNase I footprint is a TFIIIC-dependent extension of the TFIIIA footprint an additional 25 bp toward the 5' end of the gene. This indicates a direct interaction between Xenopus TFIIIC and the template DNA.