Tom Rapoport

Tom Rapoport, Ph.D.

Don W. Fawcett Professor of Cell Biology (HMS)
HHMI Investigator
LHRRB 401

Tom Rapoport, Ph.D., joined the faculty at Harvard Medical School in 1995. He received his Ph.D. in Biochemistry from the Humboldt University in East-Berlin for work in enzymology. He then focused on mathematical modeling of metabolism, for which he received his second degree (Habilitation) from the same institution. Before moving to the US, he worked at the Central Institute of Molecular Biology of the Academy of Sciences of the GDR and later at the Max-Delbrueck Center for Molecular Medicine in Berlin-Buch. In 1997, he became a Howard Hughes Medical Institute Investigator.

The Rapoport Lab is interested in the mechanisms by which proteins are transported across membranes, how misfolded proteins are degraded, and how organelles form and maintain their characteristic shapes. Most of the projects center around the endoplasmic reticulum (ER). One project concerns the molecular mechanism by which proteins are translocated across the ER membrane or across the plasma membrane in bacteria and archaea. Much of the current work deals with ERAD (ER-associated protein degradation), a process in which misfolded proteins are retro-translocated across the ER membrane into the cytosol. Major questions concern the mechanism by which proteins move across the membrane and are extracted by the Cdc48 ATPase. Another project concerns the mechanism by which ER morphology, specifically the tubular ER network, is generated. More recently, the Rapoport lab has started to study how proteins are imported into peroxisomes, and how lung surfactant proteins generate lamellar bodies. The lab employs a variety of different techniques, including biochemical methods, such as reconstitutions with purified proteins, and structural biology methods, including X-ray crystallography and cryo-electron microscopy.

Harvard Medical School

Dept. of Cell Biology, LHRRB 401

240 Longwood Avenue

Boston, MA 02115

Lab phone: 617-432-1612

The ATPase SpoIIIE transports DNA across fused septal membranes during sporulation in Bacillus subtilis.
Authors: Authors: Burton BM, Marquis KA, Sullivan NL, Rapoport TA, Rudner DZ.
Cell
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Ribosome binding of a single copy of the SecY complex: implications for protein translocation.
Authors: Authors: Ménétret JF, Schaletzky J, Clemons WM, Osborne AR, Skånland SS, Denison C, Gygi SP, Kirkpatrick DS, Park E, Ludtke SJ, Rapoport TA, Akey CW.
Mol Cell
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The signal sequence coding region promotes nuclear export of mRNA.
Authors: Authors: Palazzo AF, Springer M, Shibata Y, Lee CS, Dias AP, Rapoport TA.
PLoS Biol
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Crystal structure of an unusual thioredoxin protein with a zinc finger domain.
Authors: Authors: Ye J, Cho SH, Fuselier J, Li W, Beckwith J, Rapoport TA.
J Biol Chem
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Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes.
Authors: Authors: Rapoport TA.
Nature
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Cross-linked SecA dimers are not functional in protein translocation.
Authors: Authors: Or E, Rapoport T.
FEBS Lett
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Determining the conductance of the SecY protein translocation channel for small molecules.
Authors: Authors: Saparov SM, Erlandson K, Cannon K, Schaletzky J, Schulman S, Rapoport TA, Pohl P.
Mol Cell
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The plug domain of the SecY protein stabilizes the closed state of the translocation channel and maintains a membrane seal.
Authors: Authors: Li W, Schulman S, Boyd D, Erlandson K, Beckwith J, Rapoport TA.
Mol Cell
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Protein translocation is mediated by oligomers of the SecY complex with one SecY copy forming the channel.
Authors: Authors: Osborne AR, Rapoport TA.
Cell
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A novel dimer interface and conformational changes revealed by an X-ray structure of B. subtilis SecA.
Authors: Authors: Zimmer J, Li W, Rapoport TA.
J Mol Biol
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