Electron microscopy studies on DNA recognition by DNA-PK.
Advances in transmission electron microscopy coupled to increasingly powerful biocomputing techniques are opening enormous possibilities to understand the structure and function of complex biological processes performed by large multi-protein assemblies. This is an exciting time for electron microscopists because we can combine our efforts with X-ray crystallographers and NMR spectroscopists to reach the prospect of studying the structure and dynamics of the so-called 'molecular machines'. One of these fascinating systems is the macromolecular complex formed around double-stranded DNA breaks (DSBs). Non-homologous end-joining (NHEJ) is the main DSBs repair pathway in mammalian cells, where a collection of proteins interact to rejoin two broken DNA ends. During NHEJ, DNA-dependent protein kinase (DNA-PK) binds damaged DNA with high affinity and acts as the main scaffold for other repair factors. Several studies have made use of the electron microscope to reveal the three-dimensional architecture of DNA-PK and the structural basis for the recognition of damaged DNA and the activation of DNA-PK's kinase activity.
Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas (CSIC), Ramiro de Maeztu 9, Campus Universidad Complutense, Madrid 28040, Spain. ollorca@cib.csic.es
Oscar
O
Llorca
Laurence H
LH
Pearl
D020134:Catalytic Domain; D004247:DNA / Q000032:analysis* / Q000737:chemistry; D051747:DNA-Activated Protein Kinase; D004268:DNA-Binding Proteins; D019281:Dimerization; D008854:Microscopy, Electron; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry / Q000378:metabolism*
D004268:DNA-Binding Proteins; D004247:DNA; D051747:DNA-Activated Protein Kinase; D017346:Protein Serine-Threonine Kinases