Month: February 2011
最近一个月在2.3和2.2的data2ext版本刷了好几次, 这次打算安静用一段时间…. 强迫刷机症也要控制一下, 适可而止, 不刷机, 没什么好玩的, 但也不能2,3天就刷一次…
由于CM版权问题, CM rom现在都不带google app应用, 所以现在刷机要多一步, 刷入google app, 其实也很快, 如果需要超大rom安装软件的话, sd卡的ext分区不可少, 同时要刷入支持sd2ext的补丁. 具体刷机如下:
1. 进入recovery, wipe, 将前4项彻底wipe
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Plant Cell. 2011 Feb 9;
Authors: Zhang Z, Zhang Y, Tan H, Wang Y, Li G, Liang W, Yuan Z, Hu J, Ren H, Zhang D
Multicellular organisms contain a large number of formins; however, their physiological roles in plants remain poorly understood. Here, we reveal that formin homology 5 (FH5), a type II formin mutated in rice morphology determinant (rmd), plays a crucial role in determining rice (Oryza sativa) morphology. FH5/RMD encodes a formin-like protein consisting of an N-terminal phosphatase tensin (PTEN)-like domain, an FH1 domain, and an FH2 domain. The rmd mutants display a bending growth pattern in seedlings, are stunted as adult plants, and have aberrant inflorescence (panicle) and seed shape. Cytological analysis showed that rmd mutants have severe cell elongation defects and abnormal microtubule and microfilament arrays. FH5/RMD is ubiquitously expressed in rice tissues, and its protein localization to the chloroplast surface is mediated by the PTEN domain. Biochemical assays demonstrated that recombinant FH5 protein can nucleate actin polymerization from monomeric G-actin or actin/profilin complexes, cap the barbed end of actin filaments, and bundle actin filaments in vitro. Moreover, FH5 can directly bind to and bundle microtubules through its FH2 domain in vitro. Our findings suggest that the rice formin protein FH5 plays a critical role in determining plant morphology by regulating actin dynamics and proper spatial organization of microtubules and microfilaments.