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Yong Kim

Kim, Yong I.
Assistant Professor, chemistry and environmental
370 tiernan
Yong-Ick Kim joins NJIT from the University of California, San Diego, where he is a post-doctoral researcher at the Center for Circadian Biology. Dr. Kim studies the biochemical mechanisms underlying circadian rhythms, the bodily and behavioral changes tied to the
24-hour daily cycle that are responsive to light and darkness. His research to date has focused on pinpointing the activation and inhibition of proteins integral to regulating the circadian clock and on the biochemical mechanisms that reset it. He is interested in examining disruptions such as jet-lag in order to help devise effective treatments. His research on the molecular mechanisms of the circadian clock has been published in top journals such as the Proceedings of the National Academies of Science, Cell, and Science.
Ph.D. Texas A&M University, College Station, TX 2008 (Biochemistry)
M.S. Sungkyunkwan University, Seoul, Korea 1994 (Organic Chemistry)
B.S. Sungkyunkwan University, Seoul, Korea 1992 (Chemistry)
2015 Fall
CHEM 475 Biochemistry Lab I
2016 Spring
CHEM 673 Biochemistry

The input pathway detects changes in light and dark from the environment, and synchronizes the phase of oscillator with day/night cycles. The central oscillator is encoded by three genes, kaiA, kaiB, and kaiC, whose protein products function together to generate a 24-hour rhythm of KaiC phosphorylation. KaiC has two residues (Ser431, Thr432) that can be phosphorylated and modulation of KaiC’s autokinase and autophosphatase activities generates a 24-hour period phosphorylation and dephosphorylation rhythm. KaiA activates the autophosphorylation of KaiC and KaiB attenuates KaiA’s function, resulting in KaiC dephosphorylation. The 24-hour KaiC phosphorylation rhythm is generated by timely association and dissociation amongst these three Kai proteins. The oscillator transmits the 24-hour KaiC phosphorylation signal to an output pathway resulting in the regulation of a wide variety of rhythmic behaviors including gene expression. Three genes of the output pathway have been


1. Chang YG, Cohen S, Phong C, Meyers WK, Kim YI, Tseng R, Lin J, Zhang L, Boyd J, Lee Y, Kang S, Lee D, Li S, Britt RD, Rust MJ, Golden SS, LiWang A. (2015) A protein fold switch joins the circadian oscillator to clock output in cyanobacteria. Science,349, 324-328.
2. Kim YI, Boyd JS, Espinosa J, Golden SS. (2015) Detecting KaiC phosphorylation rhythms of the cyanobacterial circadian oscillator in vitro and in vivo. Method Enzymol. 551, 153-173.
3. Kim YI, Vinyard DJ, Ananyev G, Dismukes C, Golden SS. (2012) Oxidized quinones signal onset of darkness directly to the cyanobacterial circadian oscillator. Proc. Natl. Acad. Sci. U.S.A. 109, 17765-17769. (Inaugural article)
4. Dong G*, Kim YI*, Golden SS. (2010) Simplicity and complexity in the cyanobacterial circadian clock mechanism. Curr. Opin. Genet. Dev. 20, 619-625. (* Corresponding authors, Contributed equally to this work)
5. Wood TL*, Bridwell-Rabb J*, Kim YI*, Gao T, Chang YG, LiWang A, Barondeau DP, Golden SS. (2010) The KaiA protein of the cyanobacterial circadian oscillator is modulated by a redox-active cofactor. Proc. Natl. Acad. Sci. U.S.A. 107, 5804-5809. (* Contributed equally to this work)
6. Dong G, Yang Q, Wang Q, Kim YI, Wood TL, Osteryoung KW, van Oudenaarden AGolden SS (2010) Elevated ATPase activity of KaiC applies a circadian checkpoint on cell division in Synechococcus elongatus. Cell140, 458-459.,
7. Chen Y, Kim YI, Mackey SR, Holtman CK, LiWang AC, Golden SS (2009) A novel allele of kaiA shortens circadian period and strengthens interaction of oscillator components in the cyanobacterium Synechococcus elongatus PCC 7942. J. Bacteriol.191,4392-4400.
8. Kim YI, Dong G, Carruthers CW Jr, Golden SS, LiWang AC (2008) The day/night switch in KaiC, a central oscillator component of the circadian clock of cyanobacteria. Proc. Natl. Acad. Sci. U.S.A. 105, 12825-12830.
9. Kim YI, Manalo MN, Perez LM, LiWang AC (2006) Computational and empirical trans-hydrogen bond deuterium isotope shifts suggest that N1–N3 A:U hydrogen bonds of RNA are shorter than those of A:T hydrogen bonds of DNA. J. Biomol. NMR34, 229-236.