biotech Flashcards
biotechnology terms
secondary structure of chromatin
nucleosomal interactions, chromating folding
PTM
post-translational modification
tertiary structure of chromatin
interactions between folds of chromatin (higher order)
primary structure of chromatin
nucleosome organization in the chromatin (beads on a string), which vary in nucleotide sequence, aminoacid sequence and post-translational modification of the histones
chromatin structure description
Primary, secondary and tertiary structure of chromatin.The primary structure is shown as nucleosomal arrays consisting of nucleosomes with canonical histones (shown in light blue and yellow) and combinations of different histone variants (shown in green, purple and light blue). Nucleosomes with canonical or histone variants may vary in the degree of post-translational modifications (PTMs; such as acetylation, methylation, phosphorylation, ubiquitylation and sumoylation), generating the possibility for nucleosomes with a large number of different ‘colours’. Histone variants and PTMs may affect nucleosome structure and dynamics. The spacing between nucleosomes may vary on the basis of the underlying sequence, action of chromatin-remodelling enzymes and DNA binding by other factors (for example, transcription activators). Short-range nucleosome–nucleosome interactions result in folded chromatin fibres (secondary chromatin structure, lower left panel). Fibre–fibre interactions, which are defined by long-range interactions between individual nucleosomes, are also affected by the primary structure of chromatin fibres, including PTMs, histone variants and spacing of nucleosomes. Secondary and tertiary structures are stabilized by architectural proteins, such as linker histone H1, methyl-CpG-binding protein 2 (MeCP2), heterochromatin protein 1 (HP1), high mobility group (HMG) proteins, poly(ADP-ribose) polymerase 1 (PARP1), myeloid and erythroid nuclear termination stage-specific protein (MENT), Polycomb group proteins and many others. Transitions between the different structural states are indicated by double arrows; these may be regulated by changes in patterns of PTMs, binding or displacement of architectural proteins, exchange of histone variants and chromatin-remodelling factors.
linker DNA
shord DNA segments that connect nucleosomes.
ACP
architectural chromatin protein
histone chaperone
histone-binding proteins that influence chromatin dynamics in an ATP-independent manner
molecular chaperones
guardians of the proteome that assist in protein folding and prevent the accumulation of aberrant protein conformations that can lead to proteotoxicity
bin
region of a given size or cluster in a dataset
Hi-C
high-throughput genomic and epigenomic technique to capture chromatin conformation.[1] In general, Hi-C is considered as a derivative of a series of chromosome conformation capture technologies, including but not limited to 3C (chromosome conformation capture), 4C (chromosome conformation capture-on-chip/circular chromosome conformation capture), and 5C (chromosome conformation capture carbon copy).[1][2][3][4] Hi-C comprehensively detects genome-wide chromatin interactions in the cell nucleus by combining 3C and next-generation sequencing (NGS) approaches and has been considered as a qualitative leap in C-technology (chromosome conformation capture-based technologies) development and the beginning of 3D genomics.[2][3][4]
How Hi-C works
Similar to the classic 3C technique, Hi-C measures the frequency (as an average over a cell population) at which two DNA fragments physically associate in 3D space, linking chromosomal structure directly to the genomic sequence
TAD
topologically associated domain
pairtools
tools for manipulating sequence contact data
DNA ligation
joining of two fragments of DNA by ligase, which form a phosphodiester bond between adjacent nucleotides in duplex DNA.