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Quantifying nucleoporin stoichiometry inside single nuclear pore complexes in vivo.

Abstract：

:The nuclear pore complex (NPC) is one of the largest supramolecular structures in eukaryotic cells. Its octagonal ring-scaffold perforates the nuclear envelope and features a unique molecular machinery that regulates nucleocytoplasmic transport. NPCs are composed of ~30 different nucleoporins (Nups), averaged at 8, 16 or 32 copies per NPC. This estimate has not been confirmed for individual NPCs in living cells due to the inherent difficulty of counting proteins inside single supramolecular complexes. Here we used single-molecule SPEED microscopy to directly count the copy-number of twenty-four different Nups within individual NPCs of live yeast, and found agreement as well as significant deviation from previous estimates. As expected, we counted 8 copies of four peripheral Nups and 16 copies of fourteen scaffold Nups. Unexpectedly, we counted a maximum of 16 copies of Nsp1 and Nic96, rather than 32 as previously estimated; and found only 10-15 copies of six other Nups, rather than 8 or 16 copies as expected. This in situ molecular-counting technology can test structure-function models of NPCs and other supramolecular structures in cells.

journal_name

Sci Rep

journal_title

Scientific reports

authors

Mi L,Goryaynov A,Lindquist A,Rexach M,Yang W

doi

10.1038/srep09372

subject

Has Abstract

pub_date

2015-03-23 00:00:00

pages

9372

issn

2045-2322

pii

srep09372

journal_volume

5

pub_type

杂志文章

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