Alf1p, a CLIP-170 Domain-containing Protein, Is Functionally and Physically Associated with ?-Tubulin [electronic resource]
Tubulin is a heterodimer of ?- and ?-tubulin polypeptides. Assembly of the tubulin heterodimer in vitro requires the CCT chaperonin complex, and a set of five proteins referred to as the tubulin cofactors (Tian, F., Y. Huang, H. Rommelaere, J. Vandekerckhove, C. Ampe, and N.J. Cowan. 1996. Cell. 86:...
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Language: | English |
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Washington, D.C. : Oak Ridge, Tenn. :
United States. Department of Energy. Office of Science ; Distributed by the Office of Scientific and Technical Information, U.S. Department of Energy,
1999.
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245 | 0 | 0 | |a Alf1p, a CLIP-170 Domain-containing Protein, Is Functionally and Physically Associated with ?-Tubulin |h [electronic resource] |
260 | |a Washington, D.C. : |b United States. Department of Energy. Office of Science ; |a Oak Ridge, Tenn. : |b Distributed by the Office of Scientific and Technical Information, U.S. Department of Energy, |c 1999. | ||
300 | |a Size: p. 113-124 : |b digital, PDF file. | ||
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500 | |a Published through Scitech Connect. | ||
500 | |a 01/11/1999. | ||
500 | |a "Journal ID: ISSN 0021-9525." | ||
500 | |a Feierbach, Becket ; Nogales, Eva ; Downing, Kenneth H. ; Stearns, Tim ; | ||
520 | 3 | |a Tubulin is a heterodimer of ?- and ?-tubulin polypeptides. Assembly of the tubulin heterodimer in vitro requires the CCT chaperonin complex, and a set of five proteins referred to as the tubulin cofactors (Tian, F., Y. Huang, H. Rommelaere, J. Vandekerckhove, C. Ampe, and N.J. Cowan. 1996. Cell. 86:287?296; Tian, G., S.A. Lewis, B. Feierbach, T. Stearns, H. Rommelaere, C. Ampe, and N.J. Cowan. 1997. J. Cell Biol. 138:821?832). We report the characterization of Alf1p, the yeast ortholog of mammalian cofactor B. Alf1p interacts with ?-tubulin in both two-hybrid and immunoprecipitation assays. Alf1p and cofactor B contain a single CLIP-170 domain, which is found in several microtubule-associated proteins. Mutation of the CLIP-170 domain in Alf1p disrupts the interaction with ?-tubulin. Mutations in ?-tubulin that disrupt the interaction with Alf1p map to a domain on the cytoplasmic face of ?-tubulin; this domain is distinct from the region of interaction between ?-tubulin and ?-tubulin. Alf1p-green fluorescent protein (GFP) is able to associate with microtubules in vivo, and this localization is abolished either by mutation of the CLIP-170 domain in Alf1p, or by mutation of the Alf1p-binding domain in ?-tubulin. Analysis of double mutants constructed between null alleles of ALF1 and PAC2, which encodes the other yeast ?-tubulin cofactor, suggests that Alf1p and Pac2p act in the same pathway leading to functional ?-tubulin. The phenotype of overexpression of ALF1 suggests that Alf1p can act to sequester ?-tubulin from interaction with ?-tubulin, raising the possibility that it plays a regulatory role in the formation of the tubulin heterodimer. | |
536 | |b SC0012704. | ||
650 | 7 | |a 59 basic biological sciences |2 local. | |
650 | 7 | |a Cell biology |2 local. | |
650 | 7 | |a Tubulin |2 local. | |
650 | 7 | |a Microtubule |2 local. | |
650 | 7 | |a Saccharomyces cerevisiae |2 local. | |
650 | 7 | |a Chaperonin |2 local. | |
650 | 7 | |a Clip170 |2 local. | |
650 | 7 | |a Basic biological sciences |2 local. | |
650 | 7 | |a Clip-170 |2 local. | |
710 | 2 | |a Brookhaven National Laboratory. |4 res. | |
710 | 1 | |a United States. |b Department of Energy. |b Office of Science. |4 spn. | |
710 | 1 | |a United States. |b Department of Energy. |b Office of Scientific and Technical Information |4 dst. | |
856 | 4 | 0 | |u https://www.osti.gov/servlets/purl/1625111 |z Full Text (via OSTI) |
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952 | f | f | |p Can circulate |a University of Colorado Boulder |b Online |c Online |d Online |e E 1.99:1625111 |h Superintendent of Documents classification |i web |n 1 |