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Michael Miller

Mentor: Klaas van Wijk


University of Nebraska-Lincoln – B.S. in Plant Biology, 2014-2018

Awards and Honors


  • Achieved Dean’s list recognition each semester at the University of Nebraska-Lincoln
  • Recipient of the UCARE undergraduate research scholarship at UNL 2016-2017
  • Recipient of the George Beadle Academic Scholarship at UNL
  • Inducted as a member of the Pi Alpha Xi horticulture honor society (Alpha-Gamma chapter)
  • Awarded the Presidential Life Science Fellowship to fund my first year of graduate school

Research Experience:

Laboratory Assistant
University of Nebraska-Lincoln (Harkamal Walia Lab) — January 2017 – July 2018
Worked with post-doc to uncover the function of two rice MADS-box genes

NSF REU Research Intern
Cornell Univ. (Hosted by the Boyce Thompson Institute) — June 2017 – August 2017
Researched the genetic basis of maize leaf cuticular evaporation rates and leaf area
Mentored by Dr. Meng Lin (Michael Gore Lab)

Laboratory Assistant
University of Nebraska-Lincoln (David Holding Lab) — September 2014 – May 2017
Lab/field worker and UCARE scholarship student researcher

NSF REU Research Intern
Donald Danforth Plant Science Center — May 2016 – August 2016
Developed a high-throughput method of extracting trait data from whole-plant images
Mentored by Dr. Malia Gehan and Dr. Noah Fahlgren

Current Research Activities:

The ATP-dependent caseinolytic protease (Clp) is a crucial component of proteostasis in bacteria, mitochondria, and chloroplasts. In chloroplasts, it is composed of adapters (ClpS, ClpF), AAA+ chaperone hexamers (ClpC1, 2, and ClpD), and a 350kD tetradecameric protease core. Degradation begins with substrate selection by ClpC/D, possibly aided by ClpS/ClpF, which recognize specific degrons. ClpC/D then unfold and deliver substrates into the Clp protease core for degradation. The ClpD chaperone is specifically expressed during drought stress and senescence, whereas ClpC1 and 2 are constitutively expressed.  My research aims to identify the physiological substrates of ClpD using in vivo trapping and mass spectrometry, ii) structurally characterize ClpD and its physical interactions with other Clp proteins, and iii) characterize substrate selection mechanisms by the ClpS/ClpF co-adapter system.

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