The yeast Hsp26 protein, a conserved a-crystallin small heatshock chaperone, is assembled in to oligomeric complexes, microscopically visible as distinct cytoplasmic foci. We studied at single cell resolution the dynamics of Hsp26p foci assembly, the mode of their inheritance in to progeny cells and the physiological significance of Hsp26p function. We showed that Hsp26p foci are formed upon cells' entry in to stationary phase, but upon re-entry to proliferation they are asymmetrically retained in the mother cells and are absent from the newborn daughters. Despite the fact that Hsp26p assists re-solubilization of aggregation-prone proteins it does not extend chronological life span nor does it increase the tolerance of either mother or daughters against lethal stresses. Upon sequential HSP26 inductions, newly synthesized Hsp26p is readily incorporated in pre-existing foci, generating larger in size, but similar in appearance foci. At extreme heat-shock conditions, Hsp26p foci break apart into smaller granules dispersed in both mothers and growing buds, while recovery at normal temperature results in Hsp26p foci reassembly. These results suggested that such a complicated mechanism of dynamic Hsp26p assembly and disassembly, as well as asymmetric segregation may contribute to fine tuning regulation of protein aggregates' refolding, cell fitness and survival.
Biochemical and Biophysical Research Communications – Elsevier
Published: Sep 30, 2017
It’s your single place to instantly
discover and read the research
that matters to you.
Enjoy affordable access to
over 12 million articles from more than
10,000 peer-reviewed journals.
All for just $49/month
Read as many articles as you need. Full articles with original layout, charts and figures. Read online, from anywhere.
Keep up with your field with Personalized Recommendations and Follow Journals to get automatic updates.
It’s easy to organize your research with our built-in tools.
Read from thousands of the leading scholarly journals from SpringerNature, Elsevier, Wiley-Blackwell, Oxford University Press and more.
All the latest content is available, no embargo periods.
“Hi guys, I cannot tell you how much I love this resource. Incredible. I really believe you've hit the nail on the head with this site in regards to solving the research-purchase issue.”Daniel C.
“Whoa! It’s like Spotify but for academic articles.”@Phil_Robichaud
“I must say, @deepdyve is a fabulous solution to the independent researcher's problem of #access to #information.”@deepthiw
“My last article couldn't be possible without the platform @deepdyve that makes journal papers cheaper.”@JoseServera