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Protein Complexes Characterization in Arabidopsis thaliana by Tandem Affi nity Purifi cation Coupled to Mass Spectrometry Analysis.

Bibliography:

Bigeard J, Pflieger D, Colcombet J, Gérard L, Mireau H, Heribert Hirt​​Protein Complexes Characterization in Arabidopsis thaliana by Tandem Affi nity Purifi cation Coupled to Mass Spectrometry Analysis. Methods Molecular Biology. 2014;1171:237-50. doi: 10.1007/978-1-4939-0922-3_18. PMID: 24908132

Authors:

Bigeard J, Pflieger D, Colcombet J, Gérard L, Mireau H, Heribert Hirt

Keywords:

Arabidopsis thaliana, Protein complexes , Tandem affi nity purifi cation , Mass spectrometry , Posttranslational modifi cations

Year:

2014

Abstract:

​Proteins are major elements participating in all the key functions of the cells. They rarely fulfi ll their physiological roles in an autonomous way but rather act as part of more complex cellular machines. Indeed they can bind different types of molecules (proteins, nucleic acids, metabolites, etc.), via stable or transient interactions, depending on their nature and functions. The identifi cation of the molecular partners of a given protein is hence essential to better understand its roles, regulation, and mechanisms of action. This chapter describes the use of a tandem affi nity purifi cation approach followed by mass spectrometry analysis to try to identify and characterize the proteins involved in protein complexes in Arabidopsis thaliana and decipher some mechanisms of regulation of the modules. Important elements to consider in such an approach are fi rst extensively exposed in the introduction. This technique, in combination with complementary approaches like yeast two-hybrid and bimolecular fl uorescence complementation, can be an interesting source of data to identify and characterize in vivo protein complexes. 

ISSN:

1064-3745