Chapter title |
High-Efficiency Isolation of Nuclear Envelope Protein Complexes from Trypanosomes.
|
---|---|
Chapter number | 3 |
Book title |
The Nuclear Envelope
|
Published in |
Methods in molecular biology, January 2016
|
DOI | 10.1007/978-1-4939-3530-7_3 |
Pubmed ID | |
Book ISBNs |
978-1-4939-3528-4, 978-1-4939-3530-7
|
Authors |
Samson O. Obado, Mark C. Field, Brian T. Chait, Michael P. Rout |
Editors |
Sue Shackleton, Philippe Collas, Eric C. Schirmer |
Abstract |
Functional understanding of the nuclear envelope requires the identification of its component proteins and their interactions. Trypanosomes cause human and livestock diseases worldwide but are so divergent from animals and fungi that in silico searches for homologs of proteins are frequently of low value. Here we describe a strategy for the straightforward identification of nuclear envelope proteins from trypanosomes that classifies proteins and their interaction networks in the nuclear pore complex. Milling frozen whole cells into a powder and rapid screening of buffer conditions for optimization of complex isolation is described. The method is inexpensive and potentially applicable to many organisms, providing fast access to functional information. |
Mendeley readers
Geographical breakdown
Country | Count | As % |
---|---|---|
Unknown | 28 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Researcher | 7 | 25% |
Student > Ph. D. Student | 5 | 18% |
Professor | 4 | 14% |
Student > Bachelor | 3 | 11% |
Other | 2 | 7% |
Other | 5 | 18% |
Unknown | 2 | 7% |
Readers by discipline | Count | As % |
---|---|---|
Biochemistry, Genetics and Molecular Biology | 12 | 43% |
Agricultural and Biological Sciences | 10 | 36% |
Nursing and Health Professions | 1 | 4% |
Chemistry | 1 | 4% |
Unknown | 4 | 14% |