scholarly journals Functional comparison of the WD ‐repeat domains of SPA1 and COP1 in suppression of photomorphogenesis

2021 ◽  
Author(s):  
Konstantin Kerner ◽  
Sochichiro Nagano ◽  
Annika Lübbe ◽  
Ute Hoecker
Keyword(s):  
Wd Repeat

scholarly journals Design, Synthesis, and Evaluation of WD-Repeat-Containing Protein 5 (WDR5) Degraders

2021 ◽  
Author(s):  
Anja Dölle ◽  
Bikash Adhikari ◽  
Andreas Krämer ◽  
Janik Weckesser ◽  
Nicola Berner ◽  
...  
Keyword(s):  
Design Synthesis ◽  
Wd Repeat

scholarly journals Identification of a novel nucleolar protein complex required for mitotic chromosome segregation through centromeric accumulation of Aurora B

2020 ◽  
Vol 48 (12) ◽  
pp. 6583-6596
Author(s):  
Akiko Fujimura ◽  
Yuki Hayashi ◽  
Kazashi Kato ◽  
Yuichiro Kogure ◽  
Mutsuro Kameyama ◽  
...  
Keyword(s):  
Chromosome Segregation ◽  
Protein Complex ◽  
Metaphase Plate ◽  
Nucleolar Protein ◽  
Aurora B ◽  
Mitotic Progression ◽  
Mitotic Chromosomes ◽  
Nucleolar Proteins ◽  
Chromatid Cohesion ◽  
Wd Repeat

Abstract The nucleolus is a membrane-less nuclear structure that disassembles when cells undergo mitosis. During mitosis, nucleolar factors are thus released from the nucleolus and dynamically change their subcellular localization; however, their functions remain largely uncharacterised. Here, we found that a nucleolar factor called nucleolar protein 11 (NOL11) forms a protein complex with two tryptophan-aspartic acid (WD) repeat proteins named WD-repeat protein 43 (WDR43) and Cirhin in mitotic cells. This complex, referred to here as the NWC (NOL11-WDR43-Cirhin) complex, exists in nucleoli during interphase and translocates to the periphery of mitotic chromosomes, i.e., perichromosomal regions. During mitotic progression, both the congression of chromosomes to the metaphase plate and sister chromatid cohesion are impaired in the absence of the NWC complex, as it is required for the centromeric enrichment of Aurora B and the associating phosphorylation of histone H3 at threonine 3. These results reveal the characteristics of a novel protein complex consisting of nucleolar proteins, which is required for regulating kinetochores and centromeres to ensure faithful chromosome segregation.

scholarly journals The Essential WD Repeat Protein Swd2 Has Dual Functions in RNA Polymerase II Transcription Termination and Lysine 4 Methylation of Histone H3

2004 ◽  
Vol 24 (7) ◽  
pp. 2932-2943 ◽  
Author(s):  
Hailing Cheng ◽  
Xiaoyuan He ◽  
Claire Moore
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Chromatin Modification ◽  
Histone H3 ◽  
Temperature Sensitive ◽  
Repeat Protein ◽  
Tightly Coupled ◽  
Cleavage And Polyadenylation ◽  
Wd Repeat

ABSTRACT Swd2, an essential WD repeat protein in Saccharomyces cerevisiae, is a component of two very different complexes: the cleavage and polyadenylation factor CPF and the Set1 methylase, which modifies lysine 4 of histone H3 (H3-K4). It was not known if Swd2 is important for the function of either of these entities. We show here that, in extract from cells depleted of Swd2, cleavage and polyadenylation of the mRNA precursor in vitro are completely normal. However, temperature-sensitive mutations or depletion of Swd2 causes termination defects in some genes transcribed by RNA polymerase II. Overexpression of Ref2, a protein previously implicated in snoRNA 3′ end formation and Swd2 recruitment to CPF, can rescue the growth and termination defects, indicating a functional interaction between the two proteins. Some swd2 mutations also significantly decrease global H3-K4 methylation and cause other phenotypes associated with loss of this chromatin modification, such as loss of telomere silencing, hydroxyurea sensitivity, and alterations in repression of INO1 transcription. Even though the two Swd2-containing complexes are both localized to actively transcribed genes, the allele specificities of swd2 defects suggest that the functions of Swd2 in mediating RNA polymerase II termination and H3-K4 methylation are not tightly coupled.

Mapping and Developmental Expression Analysis of the WD-Repeat Gene Preb

Genomics ◽  
2000 ◽  
Vol 63 (3) ◽  
pp. 391-399 ◽  
Author(s):  
Catherine L. Taylor Clelland ◽  
Liviu Craciun ◽  
Carter Bancroft ◽  
Thomas Lufkin
Keyword(s):  
Expression Analysis ◽  
Developmental Expression ◽  
Wd Repeat

scholarly journals WD-repeat instability and diversification of the Podospora anserina hnwd non-self recognition gene family

2010 ◽  
Vol 10 (1) ◽  
pp. 134 ◽  
Author(s):  
Damien Chevanne ◽  
Sven J Saupe ◽  
Corinne Clavé ◽  
Mathieu Paoletti
Keyword(s):  
Gene Family ◽  
Podospora Anserina ◽  
Repeat Instability ◽  
Self Recognition ◽  
Wd Repeat

scholarly journals Crystal structure of Ski8p, a WD-repeat protein with dual roles in mRNA metabolism and meiotic recombination

2009 ◽  
Vol 13 (10) ◽  
pp. 2673-2684 ◽  
Author(s):  
Zhihong Cheng ◽  
Yuying Liu ◽  
Chernhoe Wang ◽  
Roy Parker ◽  
Haiwei Song
Keyword(s):  
Crystal Structure ◽  
Meiotic Recombination ◽  
Dual Roles ◽  
Repeat Protein ◽  
Mrna Metabolism ◽  
Wd Repeat

scholarly journals Herpesviral Protein Targets a Cellular WD Repeat Endosomal Protein to Downregulate T Lymphocyte Receptor Expression

Immunity ◽  
2002 ◽  
Vol 17 (2) ◽  
pp. 221-233 ◽  
Author(s):  
Junsoo Park ◽  
Bok-Soo Lee ◽  
Joong-Kook Choi ◽  
Robert E. Means ◽  
Joonho Choe ◽  
...  
Keyword(s):  
T Lymphocyte ◽  
Receptor Expression ◽  
Protein Targets ◽  
Wd Repeat

scholarly journals The Transcriptional Regulator Hap1p (Cyp1p) Is Essential for Anaerobic or Heme-Deficient Growth of Saccharomyces cerevisiae: Genetic and Molecular Characterization of an Extragenic Suppressor that Encodes a WD Repeat Protein

Genetics ◽  
1998 ◽  
Vol 148 (2) ◽  
pp. 559-569 ◽  
Author(s):  
Yann Chantrel ◽  
Mauricette Gaisne ◽  
Claire Lions ◽  
Jacqueline Verdière
Keyword(s):  
Profile Analysis ◽  
Signal Transduction Pathway ◽  
Cysteine Residue ◽  
Sequence Comparisons ◽  
Dependent Signal ◽  
Polysome Profile ◽  
Essential Function ◽  
Wd Repeat ◽  
Extragenic Suppressors

Abstract We report here that Hap1p (originally named Cyp1p) has an essential function in anaerobic or heme-deficient growth. Analysis of intragenic revertants shows that this function depends on the amino acid preceding the first cysteine residue of the DNA-binding domain of Hap1p. Selection of recessive extragenic suppressors of a hap1−hem1− strain allowed the identification, cloning, and molecular analysis of ASC1 (Cyp1 Absence of growth Supressor). The sequence of ASC1 reveals that its ORF is interrupted by an intron that shelters the U24 snoRNA. Deletion of the intron, inactivation of the ORF, and molecular localization of the mutations show unambiguously that it is the protein and not the snoRNA that is involved in the suppressor phenotype. ASC1, which is constitutively transcribed, encodes an abundant, cytoplasmically localized 35-kD protein that belongs to the WD repeat family, which is found in a large variety of eucaryotic organisms. Polysome profile analysis supports the involvement of this protein in translation. We propose that the absence of functional Asc1p allows the growth of hap1−hem1− cells by reducing the efficiency of translation. Based on sequence comparisons, we discuss the possibility that the protein intervenes in a kinase-dependent signal transduction pathway involved in this last function.

scholarly journals Function and regulation of F‑box/WD repeat‑containing protein 7 (Review)

2020 ◽  
Vol 20 (2) ◽  
pp. 1526-1534
Author(s):  
Zheng Zhang ◽  
Qiangsheng Hu ◽  
Wenyan Xu ◽  
Wensheng  Liu ◽  
Mengqi Liu ◽  
...  
Keyword(s):  
Wd Repeat
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