Identification and characterization of Schizosaccharomyces pombe asp1(+), a gene that interacts with mutations in the Arp2/3 complex and actin.
Identification and characterization of Schizosaccharomyces pombe asp1(+), a gene that interacts with mutations in the Arp2/3 complex and actin.
复制标题
粟酒裂殖酵母 asp1( ) 的鉴定和表征，该基因与 Arp2/3 复合物和肌动蛋白中的突变相互作用。
DOI：
10.1093/genetics/152.3.895
复制
发表时间：
1999
期刊：
影响因子：
3.3
通讯作者：
Gould,KL
中科院分区：
文献类型：
--
作者：
Feoktistova,A;McCollum,D;Ohi,R;Gould,KL
Arp 2/3复合物是酵母中肌动蛋白细胞骨架的重要组成部分，并且是肌动蛋白斑块运动所必需的。为了鉴定与裂殖酵母裂殖酵母中的这种复合物相互作用的蛋白质，我们寻找裂殖酵母的高拷贝抑制子。粟酒裂殖酵母arp 3-c1突变体，并已鉴定出一种我们称之为asp 1+的突变体。asp 1+开放阅读框（ORF）预测了一个高度保守的蛋白质，其分子量为106 kD，不包含已知功能的基序，由921个氨基酸组成。asp 1+和它的表观酿酒酵母直系同源物VIP 1都不是必需基因。然而，asp 1+的中断导致改变的形态和生长特性在升高的温度和极化生长的缺陷。asp 1破坏菌株对Ca+离子和低pH条件也非常敏感。虽然Asp 1 p是不稳定的Arp 2/3复合物，也不本地化在任何离散的结构内的细胞质，asp 1中断突变体是合成致死的突变的Arp 2/3复合物，arp 3-c1和sop 2 -1的组成部分，以及与肌动蛋白，act 1 -48突变。此外，vip 1破坏菌株与las 17 Δ菌株表现出负的遗传互作。我们得出结论，Asp 1 p/Vip 1 p是重要的皮质肌动蛋白细胞骨架的功能。
The Arp2/3 complex is an essential component of the actin cytoskeleton in yeast and is required for the movement of actin patches. In an attempt to identify proteins that interact with this complex in the fission yeast Schizosaccharomyces pombe, we sought high-copy suppressors of the S. pombe arp3-c1 mutant, and have identified one, which we have termed asp1+. The asp1+open reading frame (ORF) predicts a highly conserved protein of 921 amino acids with a molecular mass of 106 kD that does not contain motifs of known function. Neither asp1+nor its apparent Saccharomyces cerevisiae ortholog, VIP1, are essential genes. However, disruption of asp1+leads to altered morphology and growth properties at elevated temperatures and defects in polarized growth. The asp1 disruption strain also is hypersensitive to Ca+ions and to low pH conditions. Although Asp1p is not stably associated with the Arp2/3 complex nor localized in any discrete structure within the cytoplasm, the asp1 disruption mutant was synthetically lethal with mutations in components of the Arp2/3 complex, arp3-c1 and sop2-1, as well as with a mutation in actin, act1-48. Moreover, the vip1 disruption strain showed a negative genetic interaction with a las17Δ strain. We conclude that Asp1p/Vip1p is important for the function of the cortical actin cytoskeleton.