A single-molecule view of DNA replication: the dynamic nature of multi-protein complexes revealed.
نویسندگان
چکیده
Recent advances in the development of single-molecule approaches have made it possible to study the dynamics of biomolecular systems in great detail. More recently, such tools have been applied to study the dynamic nature of large multi-protein complexes that support multiple enzymatic activities. In this review, we will discuss single-molecule studies of the replisome, the protein complex responsible for the coordinated replication of double-stranded DNA. In particular, we will focus on new insights obtained into the dynamic nature of the composition of the DNA-replication machinery and how the dynamic replacement of components plays a role in the regulation of the DNA-replication process.
منابع مشابه
جداسازی پروتئین LMG از بافت کبد موش و میانکنش آن با
ABSTRACT In eukaryote cells, DNA is complexed with a series of basic proteins making units of chromatin structure named nucleosomes. In addition, nonhistone proteins with different function are the components of chromatin. Among these proteins, a group with a low mobility on gel electrophoresis have been identified and named LMG. In this study a LMG protein with a molecular weigh of 160 ...
متن کاملDNA replication at the single-molecule level.
A cell can be thought of as a highly sophisticated micro factory: in a pool of billions of molecules - metabolites, structural proteins, enzymes, oligonucleotides - multi-subunit complexes assemble to perform a large number of basic cellular tasks, such as DNA replication, RNA/protein synthesis or intracellular transport. By purifying single components and using them to reconstitute molecular p...
متن کاملPCNA tool belts and polymerase bridges form during translesion synthesis
Large multi-protein complexes play important roles in many biological processes, including DNA replication and repair, transcription, and signal transduction. One of the challenges in studying such complexes is to understand their mechanisms of assembly and disassembly and their architectures. Using single-molecule total internal reflection (TIRF) microscopy, we have examined the assembly and d...
متن کاملSingle-Molecule Studies of Origin Licensing Reveal Mechanisms Ensuring Bidirectional Helicase Loading
Loading of the ring-shaped Mcm2-7 replicative helicase around DNA licenses eukaryotic origins of replication. During loading, Cdc6, Cdt1, and the origin-recognition complex (ORC) assemble two heterohexameric Mcm2-7 complexes into a head-to-head double hexamer that facilitates bidirectional replication initiation. Using multi-wavelength single-molecule fluorescence to monitor the events of helic...
متن کاملIn vitro Delivery of HIV-1 Nef Antigen by Histidine-rich nona-arginine and Latarcin 1 peptide
Introduction: The Nef accessory protein is an attractive antigenic candidate in the development of HIV-1 DNA- or protein-based vaccines. The most crucial disadvantage of DNA and protein-based vaccines is their low immunogenicity, which can be improved by cell-penetrating peptides (CPPs) as effective carrier molecules. Methods: In this study, the HIV-1 Nef protein was generated in the Escherichi...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- Current opinion in structural biology
دوره 23 5 شماره
صفحات -
تاریخ انتشار 2013