High-Throughput Yeast Two-Hybrid Screening of Complex cDNA Libraries

Author(s):  
Kerstin Mohr ◽  
Manfred Koegl
2012 ◽  
Author(s):  
Stephan Polterauer ◽  
Dharmarao Thapi ◽  
Nikolaus Schultz ◽  
Ouathek Ouerfelli ◽  
Nancy Chen ◽  
...  

2012 ◽  
Vol 58 ◽  
pp. 245-252 ◽  
Author(s):  
Coralie Damon ◽  
Julia Dmitrieva ◽  
Yordan Muhovski ◽  
Frédéric Francis ◽  
Laurence Lins ◽  
...  

Author(s):  
George G. Roberts ◽  
Jodi R. Parrish ◽  
Bernardo A. Mangiola ◽  
Russell L. Finley

2009 ◽  
Vol 390 (1) ◽  
pp. 29-37 ◽  
Author(s):  
Jun Chen ◽  
Jianhong Zhou ◽  
Claire K. Sanders ◽  
John P. Nolan ◽  
Hong Cai

2007 ◽  
Vol 18 (11) ◽  
pp. 4317-4326 ◽  
Author(s):  
Hiroshi Qadota ◽  
Kristina B. Mercer ◽  
Rachel K. Miller ◽  
Kozo Kaibuchi ◽  
Guy M. Benian

By yeast two-hybrid screening, we found three novel interactors (UNC-95, LIM-8, and LIM-9) for UNC-97/PINCH in Caenorhabditis elegans. All three proteins contain LIM domains that are required for binding. Among the three interactors, LIM-8 and LIM-9 also bind to UNC-96, a component of sarcomeric M-lines. UNC-96 and LIM-8 also bind to the C-terminal portion of a myosin heavy chain (MHC), MHC A, which resides in the middle of thick filaments in the proximity of M-lines. All interactions identified by yeast two-hybrid assays were confirmed by in vitro binding assays using purified proteins. All three novel UNC-97 interactors are expressed in body wall muscle and by antibodies localize to M-lines. Either a decreased or an increased dosage of UNC-96 results in disorganization of thick filaments. Our previous studies showed that UNC-98, a C2H2 Zn finger protein, acts as a linkage between UNC-97, an integrin-associated protein, and MHC A in myosin thick filaments. In this study, we demonstrate another mechanism by which this linkage occurs: from UNC-97 through LIM-8 or LIM-9/UNC-96 to myosin.


2010 ◽  
Vol 9 (9) ◽  
pp. 1392-1396
Author(s):  
Zhu Tingheng ◽  
Wang Weixia ◽  
Wong Hann lin ◽  
Yang Xiao ◽  
Wang Kun ◽  
...  

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