KJ

@kjgoh.bsky.social

PhD | Biology enthusiast | RF in @LithgowLab at Monash | Video games addict |🏸🏀 lover |

If you check out my lab's recent work, you'll notice how much biofilm structure is destroyed by dehydration & vacuum during standard scanning electron microscopy. These are both images of P. aeruginosa PA14 #biofilm on pig lung tissue at 48h p.i: using cryoSEM retains the biofilm matrix. #MicroSky

In the standard SEM image, aggregates of bacterial cells with no visible matrix sit on top of a network of collagen fibrils. In the cryo image, interconnected aggregates are covered with a smooth coat of matrix, and no collagen is visible - it is under the aggregates, and the only tissue structures visible are patches of elastin fibres.

Zhi-Soon and Jacob also found that the AsmA sf protein YhdP interacts stably/specifically with DedD, which binds cell wall primarily at the division site. We offer some prelim thoughts for why/when this interaction might occur, despite seemingly distinct localization patterns. Lots to think abt! 3/3

New paper alert 🚨 I am super happy about it, for many reasons! 👥 It was a great collaborative project with Calum @chgjohnston.bsky.social and J. Pablo Radicella, designed a long time ago (in the pre-AlphaFold era - can you imagine?) together with @polardlab.bsky.social and @raphguerois.bsky.social

Calum H. G. Johnston@chgjohnston.bsky.social · 9mo ago

Pleased to share our recent article in PNAS - a collaboration with @jessicaandreani.bsky.social & Pablo Radicella, with important roles played by many members of each team. A tripartite protein complex promotes DNA transport during natural transformation in Firmicutes www.pnas.org/doi/10.1073/...

📢 𝙰𝚋𝚜𝚝𝚛𝚊𝚌𝚝 𝚂𝚞𝚋𝚖𝚒𝚜𝚜𝚒𝚘𝚗𝚜 𝙲𝚕𝚘𝚜𝚒𝚗𝚐 𝚂𝚘𝚘𝚗!! 𝙳𝚘𝚗’𝚝 𝚖𝚒𝚜𝚜 𝚢𝚘𝚞𝚛 𝚌𝚑𝚊𝚗𝚌𝚎 𝚝𝚘 𝚜𝚑𝚊𝚛𝚎 𝚢𝚘𝚞𝚛 𝚛𝚎𝚜𝚎𝚊𝚛𝚌𝚑 𝚊𝚝 𝚝𝚑𝚎 𝙻𝚘𝚛𝚗𝚎 𝙿𝚛𝚘𝚝𝚎𝚒𝚗 𝙲𝚘𝚗𝚏𝚎𝚛𝚎𝚗𝚌𝚎 𝟸𝟶𝟸𝟼. 𝙰𝚋𝚜𝚝𝚛𝚊𝚌𝚝 𝚜𝚞𝚋𝚖𝚒𝚜𝚜𝚒𝚘𝚗𝚜 𝚌𝚕𝚘𝚜𝚎 𝟸𝟺𝚝𝚑 𝙾𝚌𝚝𝚘𝚋𝚎𝚛 – 𝚜𝚑𝚘𝚠𝚌𝚊𝚜𝚎 𝚢𝚘𝚞𝚛 𝚠𝚘𝚛𝚔 𝚝𝚘 𝚝𝚑𝚎 𝚐𝚕𝚘𝚋𝚊𝚕 𝚙𝚛𝚘𝚝𝚎𝚒𝚗 𝚜𝚌𝚒𝚎𝚗𝚌𝚎 𝚌𝚘𝚖𝚖𝚞𝚗𝚒𝚝𝚢 𝚒𝚗 𝚐𝚕𝚘𝚛𝚒𝚘𝚞𝚜 𝙻𝚘𝚛𝚗𝚎! 🏖️ 🏄‍♀️ 🏊 👉 𝚂𝚞𝚋𝚖𝚒𝚝: www.lorneproteins.org/submissions

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Cryogenic electron microscopy has been used to determine the detailed structure of an intermediate state called a “D-loop” that forms when strands of DNA are exchanged during homologous recombination. buff.ly/pZZfIso

Our paper is out in its final form! Back in April 2023, my coauthor Aleks Radakovic, then a PhD student, approached me after a talk in Chicago to ask what I thought an aminoacylated tRNA would look like if we pulled it through a @nanopore. doi.org/10.1038/s414...

Nanopore sequencing of intact aminoacylated tRNAs - Nature Communications

Accurate protein synthesis depends on aminoacylated tRNAs, but their identities have been hard to measure. Here, authors present aa-tRNA-seq, a nanopore-based method that reveals the amino acid, seque...

doi.org

one small consolation of being a 60+ year old investigator is the ability to submit to 𝘔𝘈𝘛𝘜𝘙𝘌 family journals — sure they’re low impact (for our knees) but they have an early bird special if you submit between 4:00 and 5:30 on weekdays

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In this system, bacteria detect phage infection through a sensor protein (YjbH) and respond by severing the infected part of the cell via aberrant division. The rest of the cell survives and continues growing happily, essentially, bacterial autotomy!

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🍹Sharma, Jiao et al. report glycosylation of small RNAs within #exosomes and propose a glycosylation-dependent mechanism for #RNA targeting into exosomes, which may influence intercellular communication and RNA stability in the extracellular environment. 👉https://rdcu.be/eykKY bit.ly/455vyuP

Extracellular exosomal RNAs are glyco-modified - Nature Cell Biology

Sharma, Jiao and colleagues report glycosylation of small RNAs within exosomes and propose a glycosylation-dependent mechanism for RNA targeting into exosomes, which may influence intercellular commun...

bit.ly