DNA-binding domain

with OsHsfC1a, another member of the four class C HSFs identified in rice (Arvidsson et al, 2008, p. 211). Proteins hold a well preserved N-terminal DNA- binding domains that has four β-sheets and α-helices and a highly conserved oligomerization domain also known as HR-A/B domain. Putative nuclear localization signal upstream of the oligomerization domain was found in all proteins (Gupta, Palma, & Corpas, 2016). A subcellular localization study was conducted to confirm targeting of OsHsfC1b to the

a dazzling display of choreography, proteins of the the DNA mismatch repair system (MMR) come together to fix replication errors, which results in an extraordinarily high degree of genomic fidelity.1-5 It is no wonder, then, that the MMR system has transcended almost all evolutionary stratification and is a highly conserved process across species. The MMR system is chiefly responsible for initiating cellular responses for several types of DNA lesions, including single-base mismatches and small insertion-deletion

DNA repair in motion: The mechanical basis of transcription-coupled repair in prokaryotes Proper gene expression is crucial for normal physiological development. Unfortunately, the structural and functional integrity of cellular DNA is constantly at risk by intrinsic and extrinsic factors, from mistakes in metabolic processes to radiation damage. DNA repair pathways are critical processes that address these offenses by maintaining the level genomic integrity necessary for accurate cellular division

INTRODUCTION The first genome editing methods Science has led to the discovery of DNA and then identification of specific genes in organisms that control heredity and determine a cell 's function. With the advancement of research we are now able to explore the different roles of genes and understand how they might be correlated with diseases. Different approaches have been developed in order to understand the function of these genes. The first methods involved random integration of short hairpin

Unraveling the molecular mechanism of DNA binding by Transcription-activator like effectors Sequence-specific DNA targeting of nucleases, recombinases and transcriptional activators is a powerful tool to manipulate the sequence or regulate the expression of the gene of interest. While Zinc fingers specific to DNA trinucleotides, coupled to different effector domains have been employed for targeted manipulation of the genome with considerable success, we are limited by the off-target toxicity

The concept of protein domains and motifs has dominated the first half of this course. Discuss the relevance of protein domains to the following topics: a) binding of proteins to DNA Domains are parts of proteins that have some known structure and functionality. Therefore, DNA binding are stretches of a protein that contains some known structural motif and has a high affinity for DNA allowing the two to bind. One example of a proteins domain that binds DNA is the zinc finger which appear

In the spot assay, p53 mutant T155N was tested for binding by the color it develops. On the high adenine agar plate, the p53 strains, wild type (wt), mutant T155N (mut), and deletion (del), produced white cultures with all p53 response element (RE) sites, consensus (con), p21, and BAX. Therefore, all p53 strains showed transactivation because there was already enough ADE2 protein on the plate (see Figure 1B). Unlike the high adenine agar plate, the low adenine agar plate showed significant differences

of expression to unlinked genes due to DNA damage (also known as the SOS response), and mutagenesis. Within this gamut of processes in which RecA aids, the protein is specifically needed to drive three biochemical actions: interchanging homologous DNA, processing effector proteins for the SOS induction, and communicating between mutagenic proteins factors to drive synthesis past DNA lesions. Homologous recombination, the process in which double stranded DNA split and recombine between segments by

eukaryotes and their viruses. Some of the properties that make yeast suitable for studies include the existence of both stable haploids and diploids, rapid growth, clonability, and the ease of replica plating and mutant isolation. The development of DNA transformation has made yeast particularly accessible to gene cloning and genetic engineering techniques. Plasmids can be introduced into yeast cells either as replicating molecules

POT1-TPP1 heterodimer and its functions TPP1 is identified as a bridge protein in the shelterin where it binds with POT1 with the PBD, and bind with TIN2 with its CTD-CC22 domain. The interaction between TPP1 and other shelterin protein is revealed using the Oxytricha Nova telomere end binding proteins (TEBP). In O. Nova, TEBP has two heterodimers TEBP-α and TEBP-β that cap the ends of the chromosomes [13]. The TEBP-α is the homologue unit of the human POT1demostrates similar sequence to mammalian