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XB-ART-51540
Curr Biol October 19, 2015; 25 (20): 2663-71.

The Nuclear Proteome of a Vertebrate.

Wühr M , Güttler T , Peshkin L , McAlister GC , Sonnett M , Ishihara K , Groen AC , Presler M , Erickson BK , Mitchison TJ , Kirschner MW , Gygi SP .


Abstract
The composition of the nucleoplasm determines the behavior of key processes such as transcription, yet there is still no reliable and quantitative resource of nuclear proteins. Furthermore, it is still unclear how the distinct nuclear and cytoplasmic compositions are maintained. To describe the nuclear proteome quantitatively, we isolated the large nuclei of frog oocytes via microdissection and measured the nucleocytoplasmic partitioning of ∼9,000 proteins by mass spectrometry. Most proteins localize entirely to either nucleus or cytoplasm; only ∼17% partition equally. A protein''s native size in a complex, but not polypeptide molecular weight, is predictive of localization: partitioned proteins exhibit native sizes larger than ∼100 kDa, whereas natively smaller proteins are equidistributed. To evaluate the role of nuclear export in maintaining localization, we inhibited Exportin 1. This resulted in the expected re-localization of proteins toward the nucleus, but only 3% of the proteome was affected. Thus, complex assembly and passive retention, rather than continuous active transport, is the dominant mechanism for the maintenance of nuclear and cytoplasmic proteomes.

PubMed ID: 26441354
PMC ID: PMC4618192
Article link: Curr Biol
Grant support: [+]

Species referenced: Xenopus
Genes referenced: actb aloxe3 camkk1 cdk1 cfl1 fabp4 grhpr.1 grhpr.2 gstm1 gsto1 hbz hspa1a map2k1 mastl mdh1 melk nek1 pdk1 pfn1 pgk1 sod1 taldo1 tpi1 ttk xpo1


Article Images: [+] show captions
References [+] :
, Update on activities at the Universal Protein Resource (UniProt) in 2013. 2012, Pubmed