.png){kind=icon}
返回
Examining kinesin processivity within a general gating framework
.png){kind=icon}
OA
AI
DOI：10.7554/eLife.07403.png)
.png){kind=icon}
原文求助.png){kind=icon}
分享.png){kind=icon}
收藏
摘要
En 中文
Kinesin-1 is a dimeric motor that transports cargo along microtubules, taking 8.2-nm steps in a hand-over-hand fashion. The ATP hydrolysis cycles of its two heads are maintained out of phase by a series of gating mechanisms, which lead to processive runs averaging similar to 1 mu m. A key structural element for inter-head coordination is the neck linker (NL), which connects the heads to the stalk. To examine the role of the NL in regulating stepping, we investigated NL mutants of various lengths using single-molecule optical trapping and bulk fluorescence approaches in the context of a general framework for gating. Our results show that, although inter-head tension enhances motor velocity, it is crucial neither for inter-head coordination nor for rapid rear-head release. Furthermore, cysteine-light mutants do not produce wild-type motility under load. We conclude that kinesin-1 is primarily front-head gated, and that NL length is tuned to enhance unidirectional processivity and velocity.
Keyword:
ALTERNATING-SITE MECHANISM
NECK-LINKER
ATP HYDROLYSIS
FLUORESCENCE MICROSCOPY
DIMERIC KINESIN
CARGO TRANSPORT
MOTOR PROTEIN
ADP RELEASE
FRONT HEAD
BINDING
期刊
IF:
0
论文数:
1.8W
被引数:
16
机构
引用论文
Alternating-Site Mechanism of Kinesin-1 Characterized by Single-Molecule FRET Using Fluorescent ATP Analogues.png)
BIOPHYSICAL JOURNAL
OAAI
BIOPHYSICAL JOURNALIF3.1
OAAI分享收藏Kinesin moving through the spotlight: Single-motor fluorescence microscopy with submillisecond time resolutionBIOPHYSICAL JOURNALOAAI
BIOPHYSICAL JOURNALIF3.1
OAAI分享收藏分享收藏Role of the kinesin neck linker and catalytic core in microtubule-based motilityCURRENT BIOLOGYOAAI
CURRENT BIOLOGYIF7.5
OAAI分享收藏
查看更多内容