KAR3, a kinesin-related gene required for yeast nuclear fusion

Meluh, Pamela B.; Rose, Mark D.

doi:10.1016/0092-8674(90)90351-e

Cited by 491 publications

(511 citation statements)

References 66 publications

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“…Moreover, a mutation in the P-loop of SMY1 does not disrupt the ability of SMY1 to rescue a Myo2 mutant, nor does it mislocalize SMY1. This is true despite the observation that an analogous mutation in a more canonical kinesin strongly disrupts both function and localization (Meluh and Rose, 1990). Another member of this orphan family, Costal2 (COS2), localizes to microtubules, and binds microtubules in vitro, but this binding is ATP insensitive (Robbins et al, 1997;Sissons et al, 1997).…”

Section: Introductionmentioning

confidence: 86%

Orphan Kinesin NOD Lacks Motile Properties But Does Possess a Microtubule-stimulated ATPase Activity

Matthies

Baskin

Hawley

2001

MBoC

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NOD is a Drosophila chromosome-associated kinesin-like protein that does not fall into the chromokinesin subfamily. Although NOD lacks residues known to be critical for kinesin function, we show that microtubules activate the ATPase activity of NOD Ͼ2000-fold. Biochemical and genetic analysis of two genetically identified mutations of NOD (NOD DTW and NOD "DR2" ) demonstrates that this allosteric activation is critical for the function of NOD in vivo. However, several lines of evidence indicate that this ATPase activity is not coupled to vectorial transport, including 1) NOD does not produce microtubule gliding; and 2) the substitution of a single amino acid in the Drosophila kinesin heavy chain with the analogous amino acid in NOD results in a drastic inhibition of motility. We suggest that the microtubule-activated ATPase activity of NOD provides transient attachments of chromosomes to microtubules rather than producing vectorial transport.

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Section: Introductionmentioning

confidence: 86%

Orphan Kinesin NOD Lacks Motile Properties But Does Possess a Microtubule-stimulated ATPase Activity

Matthies

Baskin

Hawley

2001

MBoC

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“…Instead, the microtubule-dependent kinetochore movement observed with the CBF3 preparations is due to the kinesin-related molecular motor, Kar3p, which exhibits unspecific DNA binding and thus can contaminate CBF3 preparation [40]. Kar3p, which has been associated with karyogamy and mitosis [41], is a minus end-directed motor and could account for the chromosome movement at anaphase A in redundancy with other motor proteins (since Kar3p is not essential for viability). However, the co-purification of Kar3p and CBF3 appears accidental and therefore the in vivo role of Kar3p as a kinetochore-localized motor has yet to be established.…”

Section: Kinetochore-microtubule Interactionmentioning

confidence: 99%

The Saccharomyces cerevisiae kinetochore

Lechner¹,

Ortiz²

1996

FEBS Letters

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Accurate chromosome segregation is dependent on a specialized chromosomal structure, the kinetochore/centromere. The only essential constituent of the S. cerevisiae kinetochore established today is CBF3, a multisubunit complex that binds to S. cerevisiae centromere DNA. Therefore CBF3 and its four components, Cbf3a, Cbf3b, Cbf3c and Cbf3d, will form the centerpiece of this review. In addition, we will describe proteins that are putatively involved in kinetochore function specifically in the context with CBF3 interaction. Furthermore, we discuss the role of the S. cerevisiae kinetochores in a putative cell cycle checkpoint control and in microtubule attachment. Key words:Centromere; Kinetochore; CBF3; Saccharomyces cerevisiae Recent reviews that describe the S. cerevisiae kinetochore are available [1,5,6]. This review focuses on the protein components of the S. cerevisiae kinetochore. First we describe proteins that physically interact with the CEN DNA and we emphasize the analysis of CBF3 (_centromere DNA binding factor), a key component of the S. cerevisiae kinetochore. Second we describe proteins that are putatively involved in kinetochore function (as structural components or regulators) as deduced from genetic interactions with CEN DNA or CEN DNA binding proteins. Finally we discuss the role of the S. cerevisiae kinetochore as a putative cell cycle checkpoint and in microtubule interaction. CEN DNA binding proteins

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“…(23) kar3 mutants cause microtubules to become very long in vivo, evidence that its microtubuledestabilizing activity is an essential part of Kar3 function in the cell. (26) MCAK, a chromosome-associated kinesin protein required for mitosis, has been shown to depolymerize microtubules in vitro and is needed to regulate microtubule length in live cells. (24,27) The mechanism by which MCAK and related proteins depolymerize spindle fibers is not certain, although a model has been proposed that involves bending of protofilaments at microtubule ends by the motor, causing them to circularize and be released as tubulin rings (Fig.…”

Section: Introductionmentioning

confidence: 99%

Kinesin motors as molecular machines

Endow

2003

BioEssays

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SummaryMolecular motor proteins, fueled by energy from ATP hydrolysis, move along actin filaments or microtubules, performing work in the cell. The kinesin microtubule motors transport vesicles or organelles, assemble bipolar spindles or depolymerize microtubules, functioning in basic cellular processes. The mechanism by which motor proteins convert energy from ATP hydrolysis into work is likely to differ in basic ways from man-made machines. Several mechanical elements of the kinesin motors have now been tentatively identified, permitting researchers to begin to decipher the mechanism of motor function. The force-producing conformational changes of the motor and the means by which they are amplified are probably different for the plus-and minus-end kinesin motors.

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KAR3, a kinesin-related gene required for yeast nuclear fusion

Cited by 491 publications

References 66 publications

Orphan Kinesin NOD Lacks Motile Properties But Does Possess a Microtubule-stimulated ATPase Activity

Orphan Kinesin NOD Lacks Motile Properties But Does Possess a Microtubule-stimulated ATPase Activity

The Saccharomyces cerevisiae kinetochore

Kinesin motors as molecular machines

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