The GPQ-rich segment of Dictyostelium myosin IB contains an actin binding site.
The GPQ-rich segment of Dictyostelium myosin IB contains an actin binding site.
复制标题
盘基网柄菌肌球蛋白 IB 富含 GPQ 的片段含有肌动蛋白结合位点。
DOI：
10.1021/bi00174a045
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发表时间：
1994
期刊：
影响因子：
2.9
通讯作者：
Rener,B
中科院分区：
文献类型：
--
作者：
Rosenfeld,SS;Rener,B
Revised Manuscript Received December 22, 1993® abstract: Myosin I has been implicated as the motor that drives protrusion of the leading edge of motile cells. This function requires a close association with the plasma membrane and the cytoskeleton. Association with the actin cytoskeleton is mediated by an ATP-dependent binding site in the motor-containing myosin head, as well as by a second, ATP-independent actin binding site. In myosin IC fromAcanthamoeba, the ATP-independent actin binding site is located in the carboxy-terminal tail, in a domain composed of two segments. The first segment is basic and is referred to as the GPA-rich segment. The second is a highly conserved sequence called src homology region 3 (SH3), found in a variety of cytoskeletal-associated proteins. We haveused bacterially-expressed fusion proteins containing portions of Dictyostelium myosinIB to determine if the tail of this myosin I isoform also binds to actin and to establish precisely where the actin binding site is located. We have determined that the carboxy-terminal portion of the tail of Dictyostelium myosin IB can bind to actin in an ATP-independent manner and that the actin binding site is contained within residues 922-1059, correspondingto the GPA-rich segment of Acanthamoeba myosin IC. We conclude that this region contains a specific actin binding site which may be responsible for the cytoskeletal association of this myosin I isoform.
