This was Max Perutz’s motto and immediately goes to show what an optimistic person he was. Although in everyday scientific life this admirable attitude is sometimes lost, the Crossing Frontiers in Life Sciences symposium was a pleasant reminder that true and exciting new research is still thriving.
Since Perutz himself was primarily a structural biologist, several of the talks were given by crystallographers: for example, Isabella Moll from the Max F. Perutz Laboratoris (MFPL) gave an account of how E. coli can reprogramme which mRNAs in the cell are being translated by modifying both ribosomal (16S rRNA) and messenger RNAs. Their findings were corroborated by X-ray crystal structures of various ribosome components (for a review see Byrgazov et al. (2013)). Elena Conti, director of the Max Planck Institute in Munich, presented their X-ray crystal structures comparing eukaryotic and prokaryotic exosomes, the molecular machines responsible for degrading RNAs. Almost by accident I got to talk to her afterwards and when we discussed what sort of work I might want to pursue for my PhD she strongly recommended sticking to basic research, because cancer, for example, is just too complex.
Apart from structural biology another big topic was cell biology. An excellent talk, possibly my favourite, was given by Martin Hetzer (Salk Institute; but originally from Austria): they study the nuclear envelope in eukaryotic cells. One of their key findings is that the nuclear envelope can actually break down in non-dividing cells, causing contents of the nucleus and cytoplasm to mix. This research has implications for laminopathies (diseases in which the lamin genes are mutated; lamins coat the inner surface of the nucleus and provide, among other things, physical support) and various cancers, in which micronucleus formation is frequently observed. Their recent review is very readable: Hatch & Hetzer (2014).
Andrea Barta (MFPL) showed us that they have found a new type of alternative splicing (a mechanism by which freshly transcribed mRNAs can be altered to yield different mature mRNAs, which in turn leads to production of different proteins) termed exitron splicing: these “exonic introns” are spliced out of coding exons that were previously believed to always stay intact. Together these and some other lectures showed me (again) that I’m probably more a cell biologist than a hard-core biochemist (as the URL of this blog might suggest).
Two further talks were extremely interesting, although not in areas that I know much about: Alipasha Vaziri (MFPL) presented new methods and technologies (e.g. two-photon wide-field temporal focussing microscopy…) to improve neurobiological studies, for example, by being able to target and (in)activate neurons more specifically. Bojan Žagrović (MFPL), using mainly computational approaches, explained how the chemistry of DNA/RNA bases (purines and pyrimidines) correlates with that of the amino acids which make up their cognate proteins, and how this relationship could potentially explain the origin of the universal genetic code (for example: Polyansky & Zagrovic (2013)).
Lastly, CRISPR and Emmanuelle Charpentier (Helmholtz Centre for Infection Research): the first things I noticed were the endearing French accent and her vitality, despite having flown overnight from New York where she had just received the Dr. Paul Janssen award for biomedical research (together with Jennifer Doudna). Despite the fact that CRISPR is now widely used and will probably soon be tested for gene therapy, Dr Charpentier’s lab is still focussing on researching the basic mechanisms of the CRISPR/Cas9 systems. This makes perfect sense since this will enable more rational and informed use of the system as a genome-engineering tool. One of the papers she cited, however, gives a good overview of how CRISPR can also be used to reversibly change transcriptional activity at specific loci in an approach termed CRISPR interference (CRISPRi; Qi et al. (2013)).
Sadly, Renée Schroeder (MFPL) could not attend the symposium because she had broken her arm. I wish her a speedy recovery!
Richard Henderson (MRC LMB, Cambridge) gave the concluding lecture on “Max Perutz and the evolving frontiers of structural biology”. He started off by showing us some video clips of Max, which were very motivational and quite touching. In lieu of those videos here is a short glimpse into his life and how other scientists, including Richard Henderson, view him:
Richard Henderson then went on to discuss advances in electron microscopy, which is being used to solve protein structures at ever higher resolutions.
The symposium was also successful on the networking/social front: I met some nice people (and even got someone’s calling card) and might be able to visit the Center for Molecular Medicine (CeMM) in Vienna, which offers a PhD programme. Now, if after all this, you are (more) interested in Max Perutz then maybe this book, a collection of essays by him, might be worth a read:
Byrgazov K, Vesper O, Moll I (2013) Ribosome heterogeneity: another level of complexity in bacterial translation regulation. Current Opinion in Microbiology 16: 133-139
Hatch E, Hetzer M (2014) Breaching the nuclear, envelope in development and disease. Journal of Cell Biology 205: 133-141
Polyansky AA, Zagrovic B (2013) Evidence of direct complementary interactions between messenger RNAs and their cognate proteins. Nucleic Acids Research 41: 8434-8443
Qi LS, Larson MH, Gilbert LA, Doudna JA, Weissman JS, Arkin AP, Lim WA (2013) Repurposing CRISPR as an RNA-Guided Platform for Sequence-Specific Control of Gene Expression. Cell 152: 1173-1183