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J. Biol. Chem., Vol. 276, Issue 3, 2088-2097, January 19, 2001

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Residues in the 1A Rod Domain Segment and the Linker L2 Are Required for Stabilizing the A₁₁ Molecular Alignment Mode in Keratin Intermediate Filaments^*

Taraneh Mehrani, Kenneth C. Wu, Maria I. Morasso, Janine T. Bryan, Lyuben N. Marekov, David A. D. Parry^§, and Peter M. Steinert^¶

From the  Laboratory of Skin Biology, NIAMS, National Institutes of Health, Bethesda, Maryland 20892-2752 and the ^§ Institute of Fundamental Sciences, Massey University, Palmerston North, New Zealand

Both analyses of x-ray diffraction patterns of well oriented specimens of trichocyte keratin intermediate filaments (IF) and in vitro cross-linking experiments on several types of IF have documented that there are three modes of alignment of pairs of antiparallel molecules in all IF: A₁₁, A₂₂ and A₁₂, based on which parts of the major rod domain segments are overlapped. Here we have examined which residues may be important for stabilizing the A₁₁ mode. Using the K5/K14 system, we have made point mutations of charged residues along the chains and examined the propensities of equimolar mixtures of wild type and mutant chains to reassemble using as criteria: the formation (or not) of IF in vitro or in vivo; and stabilities of one- and two-molecule assemblies. We identified that the conserved residue Arg¹⁰ of the 1A rod domain, and the conserved residues Glu⁴ and Glu⁶ of the linker L2, were essential for stability. Additionally, conserved residues Lys³¹ of 1A and Asp¹ of 2A and non-conserved residues Asp/Asn⁹ of 1A, Asp/Asn³ of 2A, and Asp⁷ of L2 are important for stability. Notably, these groups of residues lie close to each other when two antiparallel molecules are aligned in the A₁₁ mode, and are located toward the ends of the overlap region. Although other sets of residues might theoretically also contribute, we conclude that these residues in particular engage in favorable intermolecular ionic and/or H-bonding interactions and thereby may play a role in stabilizing the A₁₁ mode of alignment in keratin IF.

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