Tuesday, May 25, 2010

Updates of the week

Genome wide gene deletion library of S.cereviseae has greatly facilitated the better understanding of various aspects of eukaryotic biology. Fission yeast, S.pombe quiet differs from Budding yeast  in various metabolic and structural aspects. The recent paper by Dong-Uk Kim et al, in Nature Biotechnology, report the construction and analysis of comprehensive heterozygous diploid deletion mutants.
Overwhelmingly 98.4% of the S.pombe genome was covered and analysed.

Nature Biotechnology (2010), Published online16 May 2010

This collection can now complement and assist further insight into peroxisome biogeneis and metabolism dynamics coupled with S.cereviseae gene deletion library.

The Latest issue of Biochem. Soc. Transac. Features 'Organelle Biogenesis and Positioning in Plants'.
Peroxisomes. mitochondria.. Plastid.. Nucleus… The issue is full of interesting articles.. There is so much to read!!

7th FENS Forum of European Neuroscience
Amsterdam, RAI Convention Centre
Federation of European Neuroscience Societies (FENS)
July 3-7, 2010

Two peroxisome related Posters will be presented in this event

Fanelli F. et al.
The authors report their finding on peroxisomal involvement in nervous tissues in Transgenic mouse model for Alzheimer disease.

Kunze M. et al
Authors report the identification of first brain specific peroxisomal matrix protein. Brain specific splice form of the potassium channel interacting protein 4 (KvChIP4) is a novel PTS2 protein and EFGP fusion protein is peroxisomal.

6-10 June 2010, Pacifio Yokohoma, Japan

Poster - Farmer LM et al, (from group of Prof. Bonnie Bartel)

"The lon2 protease contributes to continued matrix protein import into peroxisomes"

The authors mention in abstract that they are using forward genetic screen for lon2 suppressors to identify potential lon2 targets and/or regulators combined with biochemical approach. Lon2, is an AAA-Atpase/protease which itself is not directly involved in PTS2 processing but mutant shows accumulation of unprocessed PTS2 proteins.

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