Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
CONSERVATION OF THE STRUCTURE OF KERATIN INTERMEDIATE FILAMENTS - MOLECULAR MECHANISM BY WHICH DIFFERENT KERATIN MOLECULES INTEGRATE INTO PREEXISTING KERATIN INTERMEDIATE FILAMENTS DURING DIFFERENTIATION
Autore:
STEINERT PM; MAREKOV LN; PARRY DAD;
Indirizzi:
NIAMSD,SKIN BIOL BRANCH,BLDG 6,ROOM 425,9000 ROCKVILLE PIKE BETHESDA MD 20892 MASSEY UNIV,DEPT PHYS & BIOPHYS PALMERSTON NORTH NEW ZEALAND
Titolo Testata:
Biochemistry
fascicolo: 38, volume: 32, anno: 1993,
pagine: 10046 - 10056
SICI:
0006-2960(1993)32:38<10046:COTSOK>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
MOUSE EPIDERMAL-CELLS; COILED-COIL; INVITRO; CYTOKERATINS; POLYPEPTIDES; HETERODIMER; NETWORKS; DYNAMICS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
52
Recensione:
Indirizzi per estratti:
Citazione:
P.M. Steinert et al., "CONSERVATION OF THE STRUCTURE OF KERATIN INTERMEDIATE FILAMENTS - MOLECULAR MECHANISM BY WHICH DIFFERENT KERATIN MOLECULES INTEGRATE INTO PREEXISTING KERATIN INTERMEDIATE FILAMENTS DURING DIFFERENTIATION", Biochemistry, 32(38), 1993, pp. 10046-10056

Abstract

During development and differentiation, the intermediate filament component of the cytoskeleton of many cells and tissues is rebuilt by a dynamic exchange process in which one set of protein chains is replacedby another, without recourse to creation of a new network. One major example is the replacement of keratin 5/keratin 14 (K5/K14) keratin intermediate filaments (KIFs) by K1/K10 KIFs during terminal differentiation in the epidermis. The present work was undertaken to explore how this may occur. We have induced lysine-lysine cross-links with disulfosuccinimidyl tartrate in K5/K14 KIFs in order to determine the axial dimensions and relative axial alignments of the K5/K14 molecules. Many of the cross-links induced in subfilamentous oligomers containing one,two, or three molecules were also found in the intact KIF, indicatingthat the body of data thus generated provides physiologically relevant information on the structural organization in the KIF. A least-squares analysis using as data the positions of lysine residues involved in23 induced cross-links has allowed the axial alignments of the various coiled-coil segments in the rod domain to be determined. Three modesof antiparallel alignment of two neighboring molecules were found: A11 (staggered by -16.7 nm), A22 (staggered by 28.8 nm), and A12 (almostin register; staggered by only 0.3 nm). Since the axial repeat lengthis about 1 nm less than the molecular length, the data require a fourth mode of molecule alignment, termed A(CN), in which similarly directed molecules are overlapped by the equivalent of about 5-10 residues. Interestingly, these axial alignments and dimensions are essentially identical to those adduced previously for K1/K10 KIF [Steinert, P. M., Marekov, L. N., Fraser, R. D. B., & Parry, D. A. D. (1993) J. Mol. Biol. 230, 436-452], thus indicating that the two types of KIF have conserved structures. Accordingly, our new data suggest that exchange of the K5/K14 molecules by K1/K10 molecules can occur simply because both have the same linear dimensions and axial configurations. Further work will be necessary to determine whether the lack of assembly compatibility of molecules in other IF systems is due to variations in their axial dimensions and alignments.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/04/20 alle ore 07:15:19