Search for protein partners of mitochondrial single-stranded DNA-binding protein Rim1p using a yeast two-hybrid system

2003 ◽  
Vol 48 (2) ◽  
pp. 183-188 ◽  
Author(s):  
B. Kucejová ◽  
F. Foury
Keyword(s):  
Dna Binding ◽  
Hybrid System ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Yeast Two Hybrid ◽  
Single Stranded Dna ◽  
Yeast Two Hybrid System ◽  
Protein Partners ◽  
Two Hybrid

Use of yeast two-hybrid system for detection ofBacillus subtilis FtsZ protein partners

2001 ◽  
Vol 46 (4) ◽  
pp. 292-296 ◽  
Author(s):  
P. Prepiak ◽  
Z. Chromíková ◽  
I. Barák
Keyword(s):  
Hybrid System ◽  
Yeast Two Hybrid ◽  
Ofbacillus Subtilis ◽  
Yeast Two Hybrid System ◽  
Ftsz Protein ◽  
Protein Partners ◽  
Two Hybrid

LaXp180, a mammalian ActA-binding protein, identified with the yeast two-hybrid system, co-localizes with intracellular Listeria monocytogenes

2000 ◽  
Vol 2 (2) ◽  
pp. 101-114 ◽  
Author(s):  
Thilo Pfeuffer ◽  
Werner Goebel ◽  
Julia Laubinger ◽  
Michael Bachmann ◽  
Michael Kuhn
Keyword(s):  
Listeria Monocytogenes ◽  
Hybrid System ◽  
Binding Protein ◽  
Yeast Two Hybrid ◽  
Yeast Two Hybrid System ◽  
Two Hybrid

scholarly journals Steroidogenic Acute Regulatory Protein-binding Protein Cloned by a Yeast Two-hybrid System

2003 ◽  
Vol 278 (43) ◽  
pp. 42487-42494 ◽  
Author(s):  
Teruo Sugawara ◽  
Hiroshi Shimizu ◽  
Nobuhiko Hoshi ◽  
Ayako Nakajima ◽  
Seiichiro Fujimoto
Keyword(s):  
Protein Binding ◽  
Hybrid System ◽  
Binding Protein ◽  
Regulatory Protein ◽  
Steroidogenic Acute Regulatory Protein ◽  
Yeast Two Hybrid ◽  
Yeast Two Hybrid System ◽  
Steroidogenic Acute Regulatory ◽  
Two Hybrid

scholarly journals Genetic Analysis of nif Regulatory Genes by Utilizing the Yeast Two-Hybrid System Detected Formation of a NifL-NifA Complex That Is Implicated in Regulated Expression of nif Genes

1999 ◽  
Vol 181 (20) ◽  
pp. 6535-6539 ◽  
Author(s):  
Shi Lei ◽  
Lakshmidevi Pulakat ◽  
Narasaiah Gavini
Keyword(s):  
Dna Binding ◽  
Hybrid System ◽  
Transcriptional Activation ◽  
Catalytic Domain ◽  
Dna Binding Domain ◽  
Yeast Two Hybrid ◽  
Activation Domain ◽  
Yeast Two Hybrid System ◽  
Dna Fragment ◽  
Two Hybrid

ABSTRACT In diazotrophic organisms, nitrogenase synthesis and activity are tightly regulated. Two genes, nifL and nifA, are implicated as playing a major role in this regulation. NifA is a transcriptional activator, and its activity is inhibited by NifL in response to availability of excess fixed nitrogen and high O2 tension. It was postulated that NifL binds to NifA to inhibit NifA-mediated transcriptional activation of nifgenes. Mutational analysis combined with transcriptional activation studies clearly is in agreement with the proposal that NifL interacts with NifA. However, several attempts to identify NifA-NifL interactions by using methods such as coimmunoprecipitations and chemical cross-linking experiments failed to detect direct interactions between these proteins. Here we have taken a genetic approach, the use of a yeast two-hybrid protein-protein interaction assay system, to investigate NifL interaction with NifA. A DNA fragment corresponding to the kinase-like domain of nifL was PCR amplified and was used to generate translation fusions with the DNA binding domain and the DNA activation domain of the yeast transcriptional activator GAL4 in yeast two-hybrid vectors. Similarly, a DNA fragment corresponding to the catalytic domain of nifA was PCR amplified and used to generate translation fusions with the DNA-binding domain and the DNA-activation domain of GAL4 in yeast two-hybrid vectors. After introducing appropriate plasmid combinations in yeast cells, the existance of direct interaction between NifA and NifL was analyzed with the MATCHMAKER yeast two-hybrid system by testing for the expression oflacZ and his3 genes. These analyses showed that the kinase-like domain of NifL directly interacts with the catalytic domain of NifA.

Identification of α-tubulin as an hsp105α-binding protein by the yeast two-hybrid system

2003 ◽  
Vol 286 (2) ◽  
pp. 233-240 ◽  
Author(s):  
Youhei Saito ◽  
Nobuyuki Yamagishi ◽  
Keiichi Ishihara ◽  
Takumi Hatayama
Keyword(s):  
Hybrid System ◽  
Binding Protein ◽  
Yeast Two Hybrid ◽  
Yeast Two Hybrid System ◽  
Two Hybrid

scholarly journals Studies of the Interaction between Rad52 Protein and the Yeast Single-Stranded DNA Binding Protein RPA

1998 ◽  
Vol 18 (7) ◽  
pp. 4400-4406 ◽  
Author(s):  
Sharon L. Hays ◽  
Antoine A. Firmenich ◽  
Philip Massey ◽  
Ronadip Banerjee ◽  
Paul Berg
Keyword(s):  
Dna Binding ◽  
Protein Interactions ◽  
Binding Protein ◽  
Large Subunit ◽  
Critical Role ◽  
Dna Binding Protein ◽  
Protein Protein Interactions ◽  
Single Stranded Dna ◽  
Mutant Proteins ◽  
Two Hybrid

ABSTRACT The RFA1 gene encodes the large subunit of the yeast trimeric single-stranded DNA binding protein replication protein A (RPA), which is known to play a critical role in DNA replication. ASaccharomyces cerevisiae strain carrying therfa1-44 allele displays a number of impaired recombination and repair phenotypes, all of which are suppressible by overexpression of RAD52. We demonstrate that a rad52 mutation is epistatic to the rfa1-44 mutation, placingRFA1 and RAD52 in the same genetic pathway. Furthermore, two-hybrid analysis indicates the existence of interactions between Rad52 and all three subunits of RPA. The nature of this Rad52-RPA interaction was further explored by using two different mutant alleles of rad52. Both mutations lie in the amino terminus of Rad52, a region previously defined as being responsible for its DNA binding ability (U. H. Mortenson, C. Beudixen, I. Sunjeuaric, and R. Rothstein, Proc. Natl. Acad. Sci. USA 93:10729–10734, 1996). The yeast two-hybrid system was used to monitor the protein-protein interactions of the mutant Rad52 proteins. Both of the mutant proteins are capable of self-interaction but are unable to interact with Rad51. The mutant proteins also lack the ability to interact with the large subunit of RPA, Rfa1. Interestingly, they retain their ability to interact with the medium-sized subunit, Rfa2. Given the location of the mutations in the DNA binding domain of Rad52, a model incorporating the role of DNA in the protein-protein interactions involved in the repair of DNA double-strand breaks is presented.

Identifications of DNA Sequences Encoding Key Region of SCR Interacting with SRK Extracellular Domain by Using Yeast Two-Hybrid System

2013 ◽  
Vol 38 (9) ◽  
pp. 1583-1591
Author(s):  
Li-Yan XUE ◽  
Bing LUO ◽  
Li-Quan ZHU ◽  
Yong-Jun YANG ◽  
He-Cui ZHANG ◽  
...  
Keyword(s):  
Hybrid System ◽  
Dna Sequences ◽  
Extracellular Domain ◽  
Yeast Two Hybrid ◽  
Yeast Two Hybrid System ◽  
Two Hybrid
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