The Benefits of Being a "Buddy": Exploring the Medical Student Experience As Mentor to Minority High-School Students.

Purpose: The Aspiring Doctors Precollege Program at Ohio University Heritage College of Osteopathic Medicine serves to introduce underrepresented minority (URM) high-school students to careers in health care as well as introducing URM high-school students to medical student mentors. Each month, medical students and their student mentees connect through a variety of activities on the medical college campus. While the program has significant benefit for the mentees, it also provides professional development opportunities for the medical students as mentors. Many researchers have written on the value of mentored relationships between medical students and established physicians; however, exploring the benefits of medical student mentorship has yet to be discussed in the literature. Objectives: The primary objectives of this study are to understand medical student perceptions of being a mentor and describe the contributions to their medical education. Methods: Semistructured interviews were conducted with student mentors regarding their experiences serving in this program. These interviews were inductively coded for significant ideas, themes, and patterns. Results: A series of 12 research interviews were conducted with medical students who have participated in The Aspiring Doctors program for at least three semesters. Major themes that emerged from the analysis include the following: the importance of guidance in medicine through person-to-person mentoring, and identification of future career aspirations. Summary/Conclusions: Medical student mentors found this program to be a valuable addition to their educational experience. Mentoring URM high-school students offers pre-clinical medical students the opportunity to connect with their community and envision themselves serving as physicians in underresourced communities. Simultaneously, it provides a meaningful way of paying-it-forward during their education. Further studies can be done to track the outcomes of the medical students with respect to their designations stated while participating in this program, the role of mentorship on professional identity development, and possible effects on preventing/mitigating burnout.

Structural and functional analyses reveal the contributions of the C- and N-lobes of Argonaute protein to selectivity of RNA target cleavage.

Some gene transcripts have cellular functions as regulatory noncoding RNAs. For example, ∼23-nucleotide (nt)-long siRNAs are loaded into Argonaute proteins. The resultant ribonucleoprotein assembly, the RNA-induced silencing complex (RISC), cleaves RNAs that are extensively base-paired with the loaded siRNA. To date, base complementarity is recognized as the major determinant of specific target cleavage (or slicing), but little is known about how Argonaute inspects base pairing before cleavage. A hallmark of Argonaute proteins is their bilobal structure, but despite the significance of this structure for curtailing slicing activity against mismatched targets, the molecular mechanism remains elusive. Here, our structural and functional studies of a bilobed yeast Argonaute protein and its isolated catalytic C-terminal lobe (C-lobe) revealed that the C-lobe alone retains almost all properties of bilobed Argonaute: siRNA-duplex loading, passenger cleavage/ejection, and siRNA-dependent RNA cleavage. A 2.1 Å-resolution crystal structure revealed that the catalytic C-lobe mirrors the bilobed Argonaute in terms of guide-RNA recognition and that all requirements for transitioning to the catalytically active conformation reside in the C-lobe. Nevertheless, we found that in the absence of the N-terminal lobe (N-lobe), target RNAs are scanned for complementarity only at positions 5-14 on a 23-nt guide RNA before endonucleolytic cleavage, thereby allowing for some off-target cleavage. Of note, acquisition of an N-lobe expanded the range of the guide RNA strand used for inspecting target complementarity to positions 2-23. These findings offer clues to the evolution of the bilobal structure of catalytically active Argonaute proteins.