scholarly journals Structural and functional studies of 1) Actin interacting protein 5, a novel actin assembly regulator in Saccharomyces cerevisiae 2) CbbX, a red-type Rubisco activase in Cyanidioschyzon merolae

2018 ◽  
Author(s):  
Jialin Sun
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Rubisco Activase ◽  
Cyanidioschyzon Merolae ◽  
Actin Assembly ◽  
Interacting Protein ◽  
Functional Studies

scholarly journals Dia-Interacting Protein Modulates Formin-Mediated Actin Assembly at the Cell Cortex

2007 ◽  
Vol 17 (7) ◽  
pp. 579-591 ◽  
Author(s):  
Kathryn M. Eisenmann ◽  
Elizabeth S. Harris ◽  
Susan M. Kitchen ◽  
Holly A. Holman ◽  
Henry N. Higgs ◽  
...  
Keyword(s):  
Cell Cortex ◽  
Actin Assembly ◽  
Interacting Protein

Specific inhibition of transcriptional activity of the constitutive androstane receptor (CAR) by the splicing factor SF3a3

2008 ◽  
Vol 389 (10) ◽  
Author(s):  
Hye Jin Yun ◽  
Jungsun Kwon ◽  
Wongi Seol
Keyword(s):  
Transcriptional Activity ◽  
Constitutive Androstane Receptor ◽  
Splicing Factor ◽  
Yeast Two Hybrid ◽  
Interacting Protein ◽  
Functional Studies ◽  
Reporter Activity ◽  
Inhibitory Function ◽  
Two Hybrid ◽  
Hybrid Screening

Abstract The constitutive androstane receptor (CAR) is a member of the nuclear receptor superfamily and plays an important role in the degradation of xenobiotics in the liver. Using yeast two-hybrid screening, we identified SF3a3, a 60-kDa subunit of the splicing factor 3a complex, as a specific CAR-interacting protein. We further confirmed their interaction by both co-immunoprecipitation and GST pull-down assay. Functional studies showed that overexpression of SF3a3 inhibited the reporter activity driven by a promoter containing CAR binding sequences by up to 50%, whereas reduced expression of SF3a3 activated the same reporter activity by approximately three-fold. The inhibitory function of SF3a3 is independent of the presence of TCPOBOP, a CAR ligand. These data suggest that SF3a3 functions as a co-repressor of CAR transcriptional activity, in addition to its canonical function.

Saccharomyces cerevisiae geneISW2 encodes a microtubule-interacting protein required for premeiotic DNA replication

Yeast ◽  
2000 ◽  
Vol 16 (1) ◽  
pp. 35-47 ◽  
Author(s):  
Petra Trachtulcov� ◽  
Ivana Janatov� ◽  
Sepp D. Kohlwein ◽  
Jir� Ha?ek
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Dna Replication ◽  
Interacting Protein

scholarly journals Aggressive pituitary adenomas occurring in young patients in a large Polynesian kindred with a germline R271W mutation in the AIP gene

2009 ◽  
Vol 161 (5) ◽  
pp. 799-804 ◽  
Author(s):  
Juliet E Jennings ◽  
Marianthi Georgitsi ◽  
Ian Holdaway ◽  
Adrian F Daly ◽  
Maria Tichomirowa ◽  
...  
Keyword(s):  
Pituitary Adenomas ◽  
Index Case ◽  
Young Patients ◽  
Case Series ◽  
Pituitary Tumors ◽  
Maximum Diameter ◽  
Interacting Protein ◽  
Functional Studies ◽  
Aryl Hydrocarbon ◽  
Aip Gene

ObjectiveMutations in the aryl hydrocarbon receptor-interacting protein (AIP) were recently shown to confer a pituitary adenoma predisposition in patients with familial isolated pituitary adenomas (FIPA). We report a large Samoan FIPA kindred from Australia/New Zealand with an R271W mutation that was associated with aggressive pituitary tumors.Design and methodsCase series with germline screening of AIP and haplotype analyses among R271W families.ResultsThis previously unreported kindred consisted of three affected individuals that either presented with or had first symptoms of a pituitary macroadenoma in late childhood or adolescence. The index case, a 15-year-old male with incipient gigantism and his maternal aunt, had somatotropinomas, and the maternal uncle of the index case had a prolactinoma. All tumors were large (15, 40, and 60 mm maximum diameter) and two required transcranial surgery and radiotherapy. All three affected subjects and ten other unaffected relatives were found to be positive for a germline R271W AIP mutation. Comparison of the single nucleotide polymorphism patterns among this family and two previously reported European FIPA families with the same R271W mutation demonstrated no common ancestry.ConclusionsThis kindred exemplifies the aggressive features of pituitary adenomas associated with AIP mutations, while genetic analyses among three R271W FIPA families indicate that R271W represents a mutational hotspot that should be studied further in functional studies.

Persulfide formation on mitochondrial cysteine desulfurase: enzyme activation by a eukaryote-specific interacting protein and Fe–S cluster synthesis

2012 ◽  
Vol 448 (2) ◽  
pp. 171-187 ◽  
Author(s):  
Alok Pandey ◽  
Ramesh Golla ◽  
Heeyong Yoon ◽  
Andrew Dancis ◽  
Debkumar Pain
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Viability ◽  
Conformational Change ◽  
Active Site ◽  
Enzyme Activation ◽  
Accessory Proteins ◽  
Cysteine Desulfurase ◽  
Interacting Protein ◽  
Active Site Cysteine ◽  
Isolated Mitochondria

Cysteine desulfurases abstract sulfur from the substrate cysteine, generate a covalent persulfide on the active site cysteine of the enzyme, and then donate the persulfide sulfur to various recipients such as Fe–S clusters. In Saccharomyces cerevisiae, the Nfs1p protein is the only known cysteine desulfurase, and it forms a complex with Isd11p (Nfs1p·Isd11p). Both of these proteins are found primarily in mitochondria and both are essential for cell viability. In the present study we show, using the results of experiments with isolated mitochondria and purified proteins, that Isd11p is required for the cysteine desulfurase activity of Nfs1p. Whereas Nfs1p by itself was inactive, the Nfs1p·Isd11p complex formed persulfide and was active as a cysteine desulfurase. In the absence of Isd11p, Nfs1p was able to bind the substrate cysteine but failed to form a persulfide. Addition of Isd11p allowed Nfs1p with bound substrate to generate a covalent persulfide. We suggest that Isd11p induces an activating conformational change in Nfs1p to bring the bound substrate and the active site cysteine in proximity for persulfide formation. Thus mitochondrial Nfs1p is different from bacterial cysteine desulfurases that are active in the absence of accessory proteins. Isd11p may serve to regulate cysteine desulfurase activity in mitochondria.

scholarly journals Functional Studies on the Candidate ATPase Domains of Saccharomyces cerevisiae MutLα

2000 ◽  
Vol 20 (17) ◽  
pp. 6390-6398 ◽  
Author(s):  
Phuoc T. Tran ◽  
R. Michael Liskay
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Mismatch Repair ◽  
Conformational Changes ◽  
Atp Hydrolysis ◽  
Dna Mismatch Repair ◽  
Limited Proteolysis ◽  
Atp Binding ◽  
Dna Mismatch ◽  
Functional Studies

ABSTRACT Saccharomyces cerevisiae MutL homologues Mlh1p and Pms1p form a heterodimer, termed MutLα, that is required for DNA mismatch repair after mismatch binding by MutS homologues. Recent sequence and structural studies have placed the NH2 termini of MutL homologues in a new family of ATPases. To address the functional significance of this putative ATPase activity in MutLα, we mutated conserved motifs for ATP hydrolysis and ATP binding in both Mlh1p and Pms1p and found that these changes disrupted DNA mismatch repair in vivo. Limited proteolysis with purified recombinant MutLα demonstrated that the NH2 terminus of MutLα undergoes conformational changes in the presence of ATP and nonhydrolyzable ATP analogs. Furthermore, two-hybrid analysis suggested that these ATP-binding-induced conformational changes promote an interaction between the NH2 termini of Mlh1p and Pms1p. Surprisingly, analysis of specific mutants suggested differential requirements for the ATPase motifs of Mlh1p and Pms1p during DNA mismatch repair. Taken together, these results suggest that MutLα undergoes ATP-dependent conformational changes that may serve to coordinate downstream events during yeast DNA mismatch repair.

Solution structure of the Taf14 YEATS domain and its roles in cell growth of Saccharomyces cerevisiae

2011 ◽  
Vol 436 (1) ◽  
pp. 83-90 ◽  
Author(s):  
Wen Zhang ◽  
Jiahai Zhang ◽  
Xuecheng Zhang ◽  
Chao Xu ◽  
Xiaoming Tu
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Growth ◽  
Transcriptional Activation ◽  
Solution Structure ◽  
Protein Complexes ◽  
Domain Family ◽  
Functional Studies ◽  
C Terminus ◽  
Eukaryotic Species ◽  
Negative Role

Chromatin modifications play important roles in cellular biological process. A novel conserved domain family, YEATS, has been discovered in a variety of eukaryotic species ranging from yeasts to humans. Taf14, which is involved in a few protein complexes of chromatin remodelling and gene transcription, and is essential for keeping chromosome stability, regular cell growth and transcriptional regulation, contains a YEATS domain at its N-terminus. In the present study, we determined the solution structure of the Taf14 YEATS domain using NMR spectroscopy. The Taf14 YEATS domain adopts a global fold of an elongated β-sandwich, similar to the Yaf9 YEATS domain. However, the Taf14 YEATS domain differs significantly from the Yaf9 YEATS domain in some aspects, which might indicate different structural classes of the YEATS domain family. Functional studies indicate that the YEATS domain is critical for the function of Taf14 in inhibiting cell growth under stress conditions. In addition, our results show that the C-terminus of Taf14 is responsible for its interaction with Sth1, which is an essential component of the RSC complex. Taken together, this implies that Taf14 is involved in transcriptional activation of Saccharomyces cerevisiae and the YEATS domain of Taf14 might play a negative role in cell growth.

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