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Chentao Lin, Sheng Luan, Fuyuhiko Tamanoi
No abstract text is available yet for this article.
2016: Enzymes
D Chandran, M C Wildermuth
Recent studies have revealed that several mutualistic and parasitic biotrophic microbes induce a cell cycle variant termed the endocycle in host cells to support their growth and reproduction. Endoreduplication is a process in which cells successively replicate their genomes without mitosis resulting in an increase in nuclear DNA ploidy. Depending on the interaction, endoreduplication can support biotroph colonization and feeding structure initiation/development, and/or serve as a mechanism to support enhanced metabolic demands of the microbe...
2016: Enzymes
S K Sanyal, S Rao, L K Mishra, M Sharma, G K Pandey
At any given time and location, plants encounter a flood of environmental stimuli. Diverse signal transduction pathways sense these stimuli and generate a diverse array of responses. Calcium (Ca(2+)) is generated as a second messenger due to these stimuli and is responsible for transducing the signals downstream in the pathway. A large number of Ca(2+) sensor-responder components are responsible for Ca(2+) signaling in plants. The sensor-responder complexes calcineurin B-like protein (CBL) and CBL-interacting protein kinases (CIPKs) are pivotal players in Ca(2+)-mediated signaling...
2016: Enzymes
X Liu, S Yang, C-W Yu, C-Y Chen, K Wu
Reversible histone acetylation and deacetylation at the N-terminus of histone tails play a crucial role in regulation of gene activity. Hyperacetylation of histones relaxes chromatin structure and is associated with transcriptional activation, whereas hypoacetylation of histones induces chromatin compaction and gene repression. Histone acetylation and deacetylation are catalyzed by histone acetyltransferases (HATs) and histone deacetylases (HDACs), respectively. Emerging evidences revealed that plant HATs and HDACs play essential roles in regulation of gene expression in plant development and plant responses to environmental stresses...
2016: Enzymes
D Wang, A Fu
Mitochondria possess oxygen-consuming respiratory electron transfer chains (RETCs), and the oxygen-evolving photosynthetic electron transfer chain (PETC) resides in chloroplasts. Evolutionarily mitochondria and chloroplasts are derived from ancient α-proteobacteria and cyanobacteria, respectively. However, cyanobacteria harbor both RETC and PETC on their thylakoid membranes. It is proposed that chloroplasts could possess a RETC on the thylakoid membrane, in addition to PETC. Identification of a plastid terminal oxidase (PTOX) in the chloroplast from the Arabidopsis variegation mutant immutans (im) demonstrated the presence of a RETC in chloroplasts, and the PTOX is the committed oxidase...
2016: Enzymes
K He, Y Wu
Plants are sessile organisms exposed constantly to potential virulent microbes seeking for full pathogenesis in hosts. Different from animals employing both adaptive and innate immune systems, plants only rely on innate immunity to detect and fight against pathogen invasions. Plant innate immunity is proposed to be a two-tiered immune system including pathogen-associated molecular pattern (PAMP)-triggered immunity (PTI) and effector-triggered immunity. In PTI, PAMPs, the elicitors derived from microbial pathogens, are perceived by cell surface-localized proteins, known as pattern recognition receptors (PRRs), including receptor-like kinases (RLKs) and receptor-like proteins (RLPs)...
2016: Enzymes
E Saplaoura, F Kragler
Phloem serves as a highway for mobile signals in plants. Apart from sugars and hormones, proteins and RNAs are transported via the phloem and contribute to the intercellular communication coordinating growth and development. Different classes of RNAs have been found mobile and in the phloem exudate such as viral RNAs, small interfering RNAs (siRNAs), microRNAs, transfer RNAs, and messenger RNAs (mRNAs). Their transport is considered to be mediated via ribonucleoprotein complexes formed between phloem RNA-binding proteins and mobile RNA molecules...
2016: Enzymes
Laurie S Kaguni, Marcos Túlio Oliveira, Fuyuhiko Tamanoi
No abstract text is available yet for this article.
2016: Enzymes
C E Cameron, I M Moustafa, J J Arnold
Using poliovirus (PV) and its RNA-dependent RNA polymerase (RdRp) as our primary model system, we have advanced knowledge fundamental to the chemistry and fidelity of nucleotide addition by nucleic acid polymerase. Two fidelity checkpoints exist prior to nucleotide addition. The first toggles the enzyme between a nucleotide binding-occluded state and a nucleotide binding-competent state. The second represents an ensemble of conformational states of conserved structural motifs that permits retention of the incoming nucleotide in a state competent for phosphoryl transfer long enough for chemistry to occur...
2016: Enzymes
G L Ciesielski, M T Oliveira, L S Kaguni
Recent advances in the field of mitochondrial DNA (mtDNA) replication highlight the diversity of both the mechanisms utilized and the structural and functional organization of the proteins at mtDNA replication fork, despite the relative simplicity of the animal mtDNA genome. DNA polymerase γ, mtDNA helicase and mitochondrial single-stranded DNA-binding protein-the key replisome proteins, have evolved distinct structural features and biochemical properties. These appear to be correlated with mtDNA genomic features in different metazoan taxa and with their modes of DNA replication, although substantial integrative research is warranted to establish firmly these links...
2016: Enzymes
E M Boehm, M S Gildenberg, M T Washington
Proliferating cell nuclear antigen (PCNA) plays critical roles in many aspects of DNA replication and replication-associated processes, including translesion synthesis, error-free damage bypass, break-induced replication, mismatch repair, and chromatin assembly. Since its discovery, our view of PCNA has evolved from a replication accessory factor to the hub protein in a large protein-protein interaction network that organizes and orchestrates many of the key events at the replication fork. We begin this review article with an overview of the structure and function of PCNA...
2016: Enzymes
D Zhang, M O'Donnell
The cellular replicating machine, or "replisome," is composed of numerous different proteins. The core replication proteins in all cell types include a helicase, primase, DNA polymerases, sliding clamp, clamp loader, and single-strand binding (SSB) protein. The core eukaryotic replisome proteins evolved independently from those of bacteria and thus have distinct architectures and mechanisms of action. The core replisome proteins of the eukaryote include: an 11-subunit CMG helicase, DNA polymerase alpha-primase, leading strand DNA polymerase epsilon, lagging strand DNA polymerase delta, PCNA clamp, RFC clamp loader, and the RPA SSB protein...
2016: Enzymes
R Y Samson, S D Bell
DNA replication is fundamental to the propagation of all life on the planet. Remarkably, given the central importance for this process, two distinct core cellular DNA replication machineries have evolved. One is found in the bacterial domain of life and the other is present in Archaea and Eukarya. The archaeal machinery represents a simplified and presumably ancestral form of the eukaryotic DNA replication apparatus. As such, archaeal replication proteins have been studied extensively as models for their eukaryal counterparts...
2016: Enzymes
M Salas, M de Vega
The requirement of DNA polymerases for a 3'-hydroxyl (3'-OH) group to prime DNA synthesis raised the question about how the ends of linear chromosomes could be replicated. Among the strategies that have evolved to handle the end replication problem, a group of linear phages and eukaryotic and archaeal viruses, among others, make use of a protein (terminal protein, TP) that primes DNA synthesis from the end of their genomes. The replicative DNA polymerase recognizes the OH group of a specific residue in the TP to initiate replication that is guided by an internal 3' nucleotide of the template strand...
2016: Enzymes
A W Kulczyk, C C Richardson
The replication system of bacteriophage T7 is remarkable in that the 40,000 nucleotide genome is replicated over 100-fold in a matter of minutes. In order to accomplish this feat T7 has evolved an efficient and economical process for the replication of its DNA. The T7 replisome provides a model system to study DNA replication. Four proteins are sufficient for reconstitution of the functional replication complex, yet the assembled replisome recapitulates all the key features of more complex prokaryotic and eukaryotic systems...
2016: Enzymes
J S Lewis, S Jergic, N E Dixon
DNA replication in Escherichia coli initiates at oriC, the origin of replication and proceeds bidirectionally, resulting in two replication forks that travel in opposite directions from the origin. Here, we focus on events at the replication fork. The replication machinery (or replisome), first assembled on both forks at oriC, contains the DnaB helicase for strand separation, and the DNA polymerase III holoenzyme (Pol III HE) for DNA synthesis. DnaB interacts transiently with the DnaG primase for RNA priming on both strands...
2016: Enzymes
S Chodavarapu, J M Kaguni
The initiation of chromosomal DNA replication starts at a replication origin, which in bacteria is a discrete locus that contains DNA sequence motifs recognized by an initiator protein whose role is to assemble the replication fork machinery at this site. In bacteria with a single chromosome, DnaA is the initiator and is highly conserved in all bacteria. As an adenine nucleotide binding protein, DnaA bound to ATP is active in the assembly of a DnaA oligomer onto these sites. Other proteins modulate DnaA oligomerization via their interaction with the N-terminal region of DnaA...
2016: Enzymes
Keizo Inoue, Diana Stafforini, Fuyuhiko Tamanoi
No abstract text is available yet for this article.
2015: Enzymes
Diana M Stafforini
This chapter is focused on the role of the plasma form of platelet-activating factor-acetylhydrolase (PAF-AH), heretofore referred to as PAF-AH, in tumorigenic responses. Biochemical and other properties of this enzyme were discussed in detail in chapter "Plasma PAF-AH (PLA2G7): Biochemical Properties, Association with LDLs and HDLs, and Regulation of Expression" by Stafforini and in other chapters. Although phospholipases tend not to be drivers of tumorigenesis themselves, these enzymes and the lipid mediators whose levels they regulate interact with a variety of oncogenes and tumor suppressors [1]...
2015: Enzymes
Sonia Karabina, Ewa Ninio
PAFAH is specific for short acyl groups esterified at the sn-2 position of glycerol in phospholipids, and apart from PAF, it hydrolyzes oxidized phospholipids produced during LDL oxidation. As the majority of the plasma PAFAH activity is bound in humans to LDL, it is also called the lipoprotein-associated phospholipase A2 (Lp-PLA2), and it was associated with the proinflammatory processes in atherosclerosis. The epidemiological studies in Caucasian populations demonstrated that high PAFAH levels might be a risk factor for cardiovascular disease through generation of proinflammatory lysoPC/lysoPAF and oxidized fatty free acids and led to the development of darapladib, a reversible PAFAH inhibitor...
2015: Enzymes
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