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Titolo:
Residues in the 1A rod domain segment and the linker L2 are required for stabilizing the A(11) molecular alignment mode in keratin intermediate filaments
Autore:
Mehrani, T; Wu, KC; Morasso, MI; Bryan, JT; Marekov, LN; Parry, DAD; Steinert, PM;
Indirizzi:
NIAMS, Skin Biol Lab, NIH, Bethesda, MD 20892 USA NIAMS Bethesda MD USA 20892 S, Skin Biol Lab, NIH, Bethesda, MD 20892 USA Massey Univ, Inst Fundamental Sci, Palmerston North, New Zealand Massey Univ Palmerston North New Zealand Palmerston North, New Zealand
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 3, volume: 276, anno: 2001,
pagine: 2088 - 2097
SICI:
0021-9258(20010119)276:3<2088:RIT1RD>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
COILED-COIL; CROSS-LINKING; II KERATINS; EXPRESSION; DISEASE; HETERODIMER; MECHANISM; DISTINCT; PROTEINS; INVITRO;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
23
Recensione:
Indirizzi per estratti:
Indirizzo: Steinert, PM NIAMS, Skin Biol Lab, NIH, Bldg 6,Rm 425, Bethesda, MD 20892 USA NIAMS Bldg 6,Rm 425 Bethesda MD USA 20892 hesda, MD 20892 USA
Citazione:
T. Mehrani et al., "Residues in the 1A rod domain segment and the linker L2 are required for stabilizing the A(11) molecular alignment mode in keratin intermediate filaments", J BIOL CHEM, 276(3), 2001, pp. 2088-2097

Abstract

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: A(11), A(22), and A(12), based on which parts of the major rod domain segments are overlapped. Here we have examined which residues may be important for stabilizingthe A(11) mode. Using the K5/R14 system, we have made point mutations of charged residues along the chains and examined the propensities of equimolarmixtures 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 Arg(10)of the 1A rod domain, and the conserved residues Glu(4) and Glu(6) of the linker L2, were essential for stability. Additionally, conserved residues Lys(31) of 1A and Asp(1) of 2A and non-conserved residues Asp/Asn(9) of 1A, Asp/Asn(3) of 2A, and Asp(7) of L2 are important for stability. Notably, these groups of residues lie close to each other when two antiparallel molecules are aligned in the A(11) 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 A(11) mode of alignment in keratin IF.

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Documento generato il 04/04/20 alle ore 11:27:09