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Cautionary Tail: The Presence of an N-Terminal Tag on Dynein Light-Chain Roadblock/LC7 Affects Its Interaction with a Functional Partner

[ Vol. 14 , Issue. 3 ]

Author(s):

Jikui Song, John L. Markley, Jikui Song and John L. Markley   Pages 265 - 268 ( 4 )

Abstract:


As part of structural investigations of components of the molecular motor, dynein, we prepared the light chain, Robl1_mouse, with and without an N-terminal His-tag. We found that the His-tag introduced a spurious binding site for a second protein, IC74. We propose a molecular mechanism for functional interference by the His-tag.

Keywords:

Affinity tag, docking, dynein, NMR spectroscopy, protein dynamics, protein-protein interactions

Affiliation:

Department of Biochemistry,University of Wisconsin-Madison, 433 Babcock Drive, Madison WI 3706,USA., Department of Biochemistry,University of Wisconsin-Madison, 433 Babcock Drive, Madison WI 3706,USA.



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