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Biology subjects

Zhang, Q.-y.

Publications and source records attributed to Zhang, Q.-y..

2 recordsLinked to original sources

What drives change? Characterizing scientific self-efficacy development in undergraduate research experiences

Undergraduate research experiences (UREs) and course-based UREs (CUREs) promote students scientific self-efficacy growth. Yet, how self-efficacy develops during research is not understood. Furthermore, what students do during research varies in ways that likely affect self-efficacy development. We sought to address these knowledge gaps by collecting scientific self-efficacy data from CURE and URE students at nine universities at the beginning, middle, and end of a single term of research. We leveraged a theoretical advancement, latent state-trait theory-revised, to disaggregate the components of students self-efficacy into stable or trait-like self-efficacy and dynamic or state-like self-efficacy. We determined that students scientific self-efficacy was moderately stable during their research, with the most malleable component being beliefs in their abilities to figure out data collection and explain results. We also surveyed students [~]45 times throughout their research experience to test the extent to which research hours and types of research tasks contributed to self-efficacy development. We found that students who completed more analytic tasks experienced significantly more self-efficacy growth than students who completed other types of tasks, while time spent on research was not influential. Our results illustrate the importance of engaging students in analytic tasks during CUREs and UREs for fostering their self-efficacy development. Highlight for table of contentsUsing latent state-trait theory-revised, we found that students scientific self-efficacy was more stable than malleable over one research term. Beliefs about data collection and explaining results were most dynamic. Conducting more analytic tasks fostered self-efficacy, while the time spent and completion of other tasks had no effect.

scientific communication and education↗

Sequence specificity of an essential nuclear localization sequence in Mcm3

Proteins with nuclear localization sequences (NLSs) are directed into the cell nucleus through interactions between the NLS and importin proteins. NLSs are generally short motifs rich in basic amino acids; however, identifying NLSs can be challenging due to the lack of a universally conserved sequence. In this study, we characterized the sequence specificity of an essential and conserved NLS in Mcm3, a subunit of the replicative DNA helicase. Through mutagenesis and AlphaFold 3 (AF3) modeling, we demonstrate that the precise positioning of basic residues within the NLS is critical for nuclear transport of Mcm3 through optimal interactions with importin. Disrupting these interactions impairs the nuclear import of Mcm3, resulting in defective chromatin loading of MCM and poor cell growth. Our results provide a structure-guided framework for predicting and analyzing monopartite NLSs, which, despite lacking a single consensus sequence, retain key characteristics shared between the NLSs of Mcm3 and the SV40 large T antigen. Author SummaryTransporting proteins into and out of the cell nucleus is essential for chromosome-associated activities. Nuclear localization sequences (NLSs), short motifs rich in basic amino acids, are commonly found in nuclear proteins. NLSs work by interacting with importin, a key transport receptor responsible for recognizing and guiding NLS-containing proteins through the nuclear pore complex into the nucleus. Other than being rich in basic amino acids, NLSs generally lack a discernible consensus sequence, raising questions about how they specifically control nuclear transport through their interactions with importins. Through a detailed mutagenesis study of a conserved and essential NLS in Mcm3, a subunit of the replicative DNA helicase, we demonstrate that the use of AlphaFold 3 (AF3), alongside genetic, biochemical, and cell biological analyses, define key contacts between Mcm3s NLS and importin that are required for nuclear import of Mcm3.

microbiology↗