The Rubisco complex protein: A protein induced by fruit removal that forms a complex with ribulose-1,5-bisphosphate carboxylase/oxygenase

Planta ◽  
1994 ◽  
Vol 194 (1) ◽  
Author(s):  
StevenJ. Crafts-Brandner ◽  
MichaelE. Salvucci
Keyword(s):  
Protein A ◽  
Fruit Removal ◽  
Bisphosphate Carboxylase ◽  
Complex Protein

scholarly journals A Role for theSaccharomyces cerevisiaeRENT Complex Protein Net1 inHMRSilencing

Genetics ◽  
2002 ◽  
Vol 161 (4) ◽  
pp. 1411-1423
Author(s):  
Daniela Kasulke ◽  
Stefanie Seitz ◽  
Ann E Ehrenhofer-Murray
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein A ◽  
Rdna Locus ◽  
The Other ◽  
Central Component ◽  
Yeast Saccharomyces Cerevisiae ◽  
Sir Proteins ◽  
Complex Protein ◽  
Subtelomeric Regions

AbstractSilencing in the yeast Saccharomyces cerevisiae is known in three classes of loci: in the silent mating-type loci HML and HMR, in subtelomeric regions, and in the highly repetitive rDNA locus, which resides in the nucleolus. rDNA silencing differs markedly from the other two classes of silencing in that it requires a DNA-associated protein complex termed RENT. The Net1 protein, a central component of RENT, is required for nucleolar integrity and the control of exit from mitosis. Another RENT component is the NAD+-dependent histone deacetylase Sir2, which is the only silencing factor known to be shared among the three classes of silencing. Here, we investigated the role of Net1 in HMR silencing. The mutation net1-1, as well as NET1 expression from a 2μ-plasmid, restored repression at silencing-defective HMR loci. Both effects were strictly dependent on the Sir proteins. We found overexpressed Net1 protein to be directly associated with the HMR-E silencer, suggesting that Net1 could interact with silencer binding proteins and recruit other silencing factors to the silencer. In agreement with this, Net1 provided ORC-dependent, Sir1-independent silencing when artificially tethered to the silencer. In contrast, our data suggested that net1-1 acted indirectly in HMR silencing by releasing Sir2 from the nucleolus, thus shifting the internal competition for Sir2 from the silenced loci toward HMR.

scholarly journals CENP-C recruits M18BP1 to centromeres to promote CENP-A chromatin assembly

2011 ◽  
Vol 194 (6) ◽  
pp. 855-871 ◽  
Author(s):  
Ben Moree ◽  
Corey B. Meyer ◽  
Colin J. Fuller ◽  
Aaron F. Straight
Keyword(s):  
Chromosome Segregation ◽  
Protein A ◽  
Histone H3 ◽  
Chromatin Assembly ◽  
Nucleosome Assembly ◽  
Chromosomal Locus ◽  
C Protein ◽  
Centromere Protein A ◽  
Histone H3 Variant ◽  
Complex Protein

Eukaryotic chromosomes segregate by attaching to microtubules of the mitotic spindle through a chromosomal microtubule binding site called the kinetochore. Kinetochores assemble on a specialized chromosomal locus termed the centromere, which is characterized by the replacement of histone H3 in centromeric nucleosomes with the essential histone H3 variant CENP-A (centromere protein A). Understanding how CENP-A chromatin is assembled and maintained is central to understanding chromosome segregation mechanisms. CENP-A nucleosome assembly requires the Mis18 complex and the CENP-A chaperone HJURP. These factors localize to centromeres in telophase/G1, when new CENP-A chromatin is assembled. The mechanisms that control their targeting are unknown. In this paper, we identify a mechanism for recruiting the Mis18 complex protein M18BP1 to centromeres. We show that depletion of CENP-C prevents M18BP1 targeting to metaphase centromeres and inhibits CENP-A chromatin assembly. We find that M18BP1 directly binds CENP-C through conserved domains in the CENP-C protein. Thus, CENP-C provides a link between existing CENP-A chromatin and the proteins required for new CENP-A nucleosome assembly.

scholarly journals Shared and tailored common bean transcriptomic responses to combined fusarium wilt and water deficit

2021 ◽  
Vol 8 (1) ◽  
Author(s):  
Susana T. Leitão ◽  
Carmen Santos ◽  
Susana de Sousa Araújo ◽  
Diego Rubiales ◽  
Maria Carlota Vaz Patto
Keyword(s):  
Common Bean ◽  
Water Deficit ◽  
Fusarium Wilt ◽  
Protein A ◽  
Photosynthetic Performance ◽  
Ribulose Bisphosphate Carboxylase ◽  
Bisphosphate Carboxylase ◽  
Combined Stresses ◽  
Transcriptional Changes ◽  
Single Stress

AbstractCommon bean (Phaseolus vulgaris L.), one of the most consumed food legumes worldwide, is threatened by two main constraints that are found frequently together in nature, water deficit (WD) and fusarium wilt (Fop). To understand the shared and unique responses of common bean to Fop and WD, we analyzed the transcriptomic changes and phenotypic responses in two accessions, one resistant and one susceptible to both stresses, exposed to single and combined stresses. Physiological responses (photosynthetic performance and pigments quantification) and disease progression were also assessed. The combined FopWD imposition negatively affected the photosynthetic performance and increased the susceptible accession disease symptoms. The susceptible accession revealed a higher level of transcriptional changes than the resistant one, and WD single stress triggered the highest transcriptional changes. While 89 differentially expressed genes were identified exclusively in combined stresses for the susceptible accession, 35 were identified in the resistant one. These genes belong mainly to “stress”, “signaling”, “cell wall”, “hormone metabolism”, and “secondary metabolism” functional categories. Among the up-regulated genes with higher expression in the resistant accession, the cysteine-rich secretory, antigen 5 and Pr-1 (CAP) superfamily protein, a ribulose bisphosphate carboxylase family protein, and a chitinase A seem promising targets for multiple stress breeding.

Engineering Bioactive Surfaces with Fischer Carbene Complex: Protein A on Self-Assembled Monolayer for Antibody Sensing

2011 ◽  
Vol 22 (6) ◽  
pp. 1202-1209 ◽  
Author(s):  
Piyali Dutta ◽  
Sudeshna Sawoo ◽  
Namrata Ray ◽  
Othman Bouloussa ◽  
Amitabha Sarkar
Keyword(s):  
Protein A ◽  
Self Assembled Monolayer ◽  
Carbene Complex ◽  
Fischer Carbene ◽  
Complex Protein ◽  
Bioactive Surfaces ◽  
Self Assembled

Use of Protein a Conjugated to Peroxidase to Localize Immunoglobulin G in SSPE Ferret Brain

1982 ◽  
Vol 40 ◽  
pp. 350-351
Author(s):  
Hannah R. Brown ◽  
Anthony F. Nostro ◽  
Halldor Thormar
Keyword(s):  
Immunoglobulin G ◽  
Human Disease ◽  
Measles Virus ◽  
Subacute Sclerosing Panencephalitis ◽  
Protein A ◽  
Inflammatory Lesions ◽  
Sspe Virus ◽  
Specific Immunoglobulin ◽  
Antibody Titers ◽  
The Brain

Subacute sclerosing panencephalitis (SSPE) is a slowly progressing disease of the CNS in children which is caused by measles virus. Ferrets immunized with measles virus prior to inoculation with the cell associated, syncytiogenic D.R. strain of SSPE virus exhibit characteristics very similar to the human disease. Measles virus nucleocapsids are present, high measles antibody titers are found in the sera and inflammatory lesions are prominent in the brains. Measles virus specific immunoglobulin G (IgG) is present in the brain,and IgG/ albumin ratios indicate that the antibodies are synthesized within the CNS.

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