Search results for: Joachim Jaeger
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In bacterial systems, adaptive protein sequence changes can be mediated by diversity-generating retroelements in a process known as retrohoming. An accessory variability determinant (Avd), together with a reverse transcriptase (RT), is critically involved in this process. In this issue of Structure, Alayyoubi and colleagues describe the structure of Avd as a basis for interactions with RT that promote...
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The West Nile virus (WNV) genome contains a single RNA-dependent RNA polymerase (RdRp) gene, which is responsible for replication of the viral genome and, as such, is an important target for antiviral therapy. Viral RdRps are known to lack proofreading capabilities and as a result viruses such as WNV exist as a mixture of viral genotypes within an infection, enabling the virus to readily emerge and...
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In this issue of Structure, Golosov et al. present molecular dynamics simulations that illuminate the process of DNA translocation by an A-family DNA polymerase. Several distinct phases are identified that have not been visualized through crystallographic studies.
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DNA Repair > 2009 > 8 > 2 > 182-189
Loop II of DNA polymerase beta (pol β) consists of 14 amino acid residues and is highly flexible and solvent exposed. Previous research from our laboratory has shown that this loop is important for polymerase activity and fidelity. In the study presented here, we demonstrate that a shortened five amino acid residue loop compromises the fidelity of pol β. This five-residue loop, termed ENEYP, induces...
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FEBS Letters > 2003 > 535 > 1-3 > 34-38
Hepatitis C virus (HCV) cannot be grown in vitro, making biochemical identification of new drug targets especially important. HCV p7 is a small hydrophobic protein of unknown function, yet necessary for particle infectivity in related viruses [Harada, T. et al., (2000) J. Virol. 74, 9498-9506]. We show that p7 can be cross-linked in vivo as hexamers. Escherichia coli expressed p7 fusion proteins also...
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Folding and Design > 1997 > 2 > 6 > R93-R104
The remarkable ability of the chaperonin GroEL to recognise a diverse range of non-native states of proteins constitutes one of the most fascinating molecular recognition events in protein chemistry. Recent structural studies have revealed a possible model for substrate binding by GroEL and a high-resolution image of the GroEL–GroES folding machinery has provided important new insights into our understanding...
