Molecular, Cellular, and Developmental Biology at the University of Michigan
Molecular, Cellular, and Developmental Biology
Molecular, Cellular, and Developmental Biology

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Linda Barthel of the Raymond Lab.
Members of the Chapman Lab.
Michael O'Connor of the Chapman Lab.
Members of the Jakob Lab.

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The Department of Molecular, Cellular and Developmental Biology strives to develop new knowledge through basic research about the function of living organisms with focus on the molecular and cellular levels of all branches of life - bacteria, plants, and animals. Our faculty research strengths are animal physiology and neurobiology, biochemistry, cell biology, developmental biology, microbiology and plant molecular biology. We are home to the undergraduate concentration in Cell and Molecular Biology that graduates nearly 200 students per year. Our General Public and Pre-College Students section offers answers to questions about biology. We hope you find our site informative!
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MCDB News
Undergraduates
and their faculty adviser, Ray Barbehenn, helped explain an observation that had puzzled insect ecologists who study gypsy moth caterpillars. Read more.

MCDB News
Elaina Breznau,
a graduate student in the Miller Lab, was recently awarded a Journal of Cell Science Travelling Fellowship. Read more.

MCDB News
Lilia Popova,
a member of the Schiefelbein Lab, has been selected as a 2013 Intel Science Talent Search Finalist. Read more.

MCDB News
MCDB Professors
James Bardwell, Jianming Li, and Eran Pichersky have been named American Association for the Advancement of Science (AAAS) Fellows. Read more.

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Adnan Syed,
a PhD student in the Boles Lab, was recently awarded an American Heart Association Predoctoral Fellowship. Read more.

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Professor Emeritus
Sally Allen
passed away November 13, 2012 at age 86 after a brief illness. Sally was professor of biology for over 30 years and was a tireless and dedicated researcher and lecturer. Read more.

Read more MCDB News
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Order out of Disorder: Working Cycle of an Intrinsically Unfolded Chaperone
Cell, Volume 148, Issue 5, 947-957, 2 March 2012
Dana Reichmann, Ying Xu, Claudia M. Cremers, Marianne Ilbert, Roni Mittelman, Michael C. Fitzgerald, Ursula Jakob

The redox-regulated chaperone Hsp33 protects organisms against oxidative stress that leads to protein unfolding. Activation of Hsp33 is triggered by the oxidative unfolding of its own redox-sensor domain, making Hsp33 a member of a recently discovered class of chaperones that require partial unfolding for full chaperone activity. Here we address the long-standing question of how chaperones recognize client proteins. We show that Hsp33 uses its own intrinsically disordered regions to discriminate between unfolded and partially structured folding intermediates. Binding to secondary structure elements in client proteins stabilizes Hsp33's intrinsically disordered regions, and this stabilization appears to mediate Hsp33's high affinity for structured folding intermediates. Return to nonstress conditions reduces Hsp33's disulfide bonds, which then significantly destabilizes the bound client proteins and in doing so converts them into less-structured, folding-competent client proteins of ATP-dependent foldases. We propose a model in which energy-independent chaperones use internal order-to-disorder transitions to control substrate binding and release.

This paper was featured in the U-M News Service article "It takes two to tango: Pairs of entwined proteins handle the stress." Read this Publication Read All Featured Publications
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