两种靶向质谱方法未检测到质体钙调蛋白样蛋白和GFP融合蛋白

Elisa Dell’Aglio , Daniel Salvi , Alexandra Kraut , Mathieu Baudet , David Macherel , Martine Neveu , Myriam Ferro , Gilles Curien , Norbert Rolland
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引用次数: 4

摘要

cam样蛋白(cml)定位于细胞质和细胞器中,如线粒体、过氧化物酶体和液泡。迄今为止,虽然有几个质体蛋白被鉴定为CaM/CML相互作用物,但没有CML被分配到叶绿体上。缺乏关于质体cml遗传特性的线索阻碍了对其调控作用的研究。为了提高我们对plastidial Ca2+调控的理解,我们尝试用两种大规模的、cam特异性的蛋白质组学方法和gfp融合来鉴定plastidial cml。结论尽管使用了几种不同的方法,但仍无法确定可塑性CML。cml35、CML36和CML41的GFP融合表明其细胞质定位。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
No plastidial calmodulin-like proteins detected by two targeted mass-spectrometry approaches and GFP fusion proteins

Background

CaM-like proteins (CMLs) are localized in the cytosol and others in organelles such as the mitochondria, the peroxisomes and the vacuole. To date, although several plastidial proteins were identified as CaM/CML interactors, no CMLs were assigned to the chloroplast. Absence of clues about the genetic identity of plastidial CMLs prevents investigating their regulatory role.

Results

To improve our understanding of plastidial Ca2+ regulation, we attempted to identify plastidial CMLs with two large scale, CaM-specific proteomic approaches, and GFP-fusions.

Conclusions

Despite the use of several different approaches no plastidial CML could be identified. GFP fusion of CML 35 CML36 and CML41 indicate a cytosolic localization.

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