Recognition of a structural domain (RWDBD) in Gcn1 proteins that interacts with the RWD domain containing proteins

Biology Direct

Evelyn Sattlegger¹  Rangachari Krishnan¹  Narayanaswamy Srinivasan²  Ramachandran Rakesh² 

[1] Institute of Natural and Mathematical Sciences (INMS), Massey University;Molecular Biophysics Unit, Indian Institute of Science;

关键词: Remote relationship;    Gcn1;    Gcn2;    RWDBD;    Sequence and structure analysis;    Protein evolution and conservation;   

DOI  :  10.1186/s13062-017-0184-3

来源: DOAJ

【 摘 要 】

Abstract The protein Gcn1 (General control non-derepressible 1) is found in virtually all eukaryotes, and is a key component of the general amino acid control signal transduction pathway. This pathway is best known for its importance for cells to sense and overcome amino acid starvation. Gcn1 directly binds to the RWD (RING finger-containing proteins, WD-repeat-containing proteins, and yeast DEAD (DEXD)-like helicases) domain of the protein kinase Gcn2, and this is essential for delivering the starvation signal to Gcn2. Gcn2, and thus the GAAC (General Amino Acid Control) pathway, then becomes activated enabling the cell to cope and overcome the starvation condition. Using sensitive homology detection and fold recognition methods a conserved structural domain in Gcn1, RWD Binding Domain (RWDBD), has been recognized that encompasses the region experimentally shown previously to be involved in Gcn2 binding. Further, the structural fold for this domain has been recognized as the ARM (Armadillo) domain, and residues likely to be involved in the binding of Gcn2 RWD domain have been identified within this structural domain. Thus, the current analysis provides a structural basis of Gcn1-Gcn2 association. Reviewers This article was reviewed by Dr Oliviero Carugo and Dr Michael Gromiha.

【 授权许可】

Unknown