Molecular Cloning, and Characterization of an Adenylyl Cyclase-Associated Protein from Gossypium arboreum L.  

作　　者：WANG Sheng ZHAO Guo-hong JIA Yin-hua DU Xiong-ming 

机构地区：[1]Cotton Germplasm Division, Cotton Research Institute, Chinese Academy of Agricultural Sciences, Anyang 455000, P.R.China

出　　处：《Agricultural Sciences in China》2009年第7期777-783,共7页中国农业科学（英文版）

基　　金：supported by the support of the National Key Technology R&D Program of China(2006BAD13B04);the National Basic Research Program of China (973 Program, 2004CB117301)

摘　　要：The aim of this study was to clone CAP （adenylyl cyclase-associated protein） gene from Gossypium arboreum L. and develop a platform for expressing and purifying CAP protein, which is a base for the construction and function researches of CAP. In this work, a CAP homolog from cotton （DPL971） ovule was identified and cloned. And the cDNA sequence consisted of an open reading frame of 1 416 nucleotides encoding a protein of 471 amino acid residues with a calculated molecular weight of 50.6 kDa. To gain insight on the CAP role in cotton fiber development, the cloned CAP cDNA was expressed. A significant higher yield pure protein was obtained with the chromatographic method. Further experiments showed that the purified protein can bind with the actin in vitro indicating that the recombinant cotton CAP is functional. The procedure described here produced high yield pure protein through one chromatographic step, suitable for further structure-function studies.The aim of this study was to clone CAP （adenylyl cyclase-associated protein） gene from Gossypium arboreum L. and develop a platform for expressing and purifying CAP protein, which is a base for the construction and function researches of CAP. In this work, a CAP homolog from cotton （DPL971） ovule was identified and cloned. And the cDNA sequence consisted of an open reading frame of 1 416 nucleotides encoding a protein of 471 amino acid residues with a calculated molecular weight of 50.6 kDa. To gain insight on the CAP role in cotton fiber development, the cloned CAP cDNA was expressed. A significant higher yield pure protein was obtained with the chromatographic method. Further experiments showed that the purified protein can bind with the actin in vitro indicating that the recombinant cotton CAP is functional. The procedure described here produced high yield pure protein through one chromatographic step, suitable for further structure-function studies.

关 键 词：adenylyl cyclase-associated protein CAP cotton fiber protein expression protein purification Gossypiumarboreum L. 

分 类 号：S-03[农业科学]