@misc{liang_strickland_ye_wu_hu_rittschof_2019, title={Biochemistry of Barnacle Adhesion: An Updated Review}, volume={6}, ISSN={["2296-7745"]}, DOI={10.3389/fmars.2019.00565}, abstractNote={Barnacles are notorious marine fouling organisms, whose life cycle initiates with the planktonic larva, followed by the free-swimming cyprid that voluntarily explores and searches for an appropriate site to settle and metamorphoses into a sessile adult. Within this life cycle, both the cyprid and the adult barnacle deposit multi-protein adhesives for temporary or permanent underwater adhesion. Here, we present a comprehensive review of the biochemistries behind these different adhesion events in the life cycle of a barnacle. First, we introduce the multiple adhesion events and their corresponding adhesives from two complementary aspects: the in vivo synthesis, storage, and secretion as well as the in vitro morphology and biochemistry. The amino acid compositions, sequences, and structures of adult barnacle adhesive proteins are specifically highlighted. Second, we discuss the molecular mechanisms of adult barnacle underwater attachment in detail by analyzing the possible adhesive and cohesive roles of different adhesive proteins, and based on these analyses, we propose an update to the original barnacle underwater adhesion molecular model. We believe that this review can greatly promote the general understanding of the molecular mechanisms underlying the reversible and irreversible underwater adhesion of barnacles and their larvae. Such an understanding is the basis for the prevention of barnacle fouling on target surfaces as well as designing conceptually new barnacle-inspired artificial underwater adhesives.}, journal={FRONTIERS IN MARINE SCIENCE}, author={Liang, Chao and Strickland, Jack and Ye, Zonghuang and Wu, Wenjian and Hu, Biru and Rittschof, Dan}, year={2019}, month={Sep} }
 @article{countryman_fan_gorthi_pan_strickland_kaur_wang_lin_lei_white_et al._2018, title={Cohesin SA2 is a sequence-independent DNA-binding protein that recognizes DNA replication and repair intermediates}, volume={293}, ISSN={["1083-351X"]}, DOI={10.1074/jbc.m117.806406}, abstractNote={Proper chromosome alignment and segregation during mitosis depend on cohesion between sister chromatids, mediated by the cohesin protein complex, which also plays crucial roles in diverse genome maintenance pathways. Current models attribute DNA binding by cohesin to entrapment of dsDNA by the cohesin ring subunits (SMC1, SMC3, and RAD21 in humans). However, the biophysical properties and activities of the fourth core cohesin subunit SA2 (STAG2) are largely unknown. Here, using single-molecule atomic force and fluorescence microscopy imaging as well as fluorescence anisotropy measurements, we established that SA2 binds to both dsDNA and ssDNA, albeit with a higher binding affinity for ssDNA. We observed that SA2 can switch between the 1D diffusing (search) mode on dsDNA and stable binding (recognition) mode at ssDNA gaps. Although SA2 does not specifically bind to centromeric or telomeric sequences, it does recognize DNA structures often associated with DNA replication and double-strand break repair, such as a double-stranded end, single-stranded overhang, flap, fork, and ssDNA gap. SA2 loss leads to a defect in homologous recombination–mediated DNA double-strand break repair. These results suggest that SA2 functions at intermediate DNA structures during DNA transactions in genome maintenance pathways. These findings have important implications for understanding the function of cohesin in these pathways.}, number={3}, journal={JOURNAL OF BIOLOGICAL CHEMISTRY}, author={Countryman, Preston and Fan, Yanlin and Gorthi, Aparna and Pan, Hai and Strickland, Jack and Kaur, Parminder and Wang, Xuechun and Lin, Jiangguo and Lei, Xiaoying and White, Christian and et al.}, year={2018}, month={Jan}, pages={1054–1069} }