NUCLEUS: STRUCTURE AN FUNCTION
→DNA is the structural basics of genetic information.
→Antiparallel double helix
SUPERCOILING
→In bacteria, DNA is condensed into supercoiled structures.
→Supercoiling effectively decreases the length of the chromosome.
→Positive supercoiled occur in the direction of the double helix, which tightens DNA (properly written of 8 ). Tight coil.
→Negative supercoils occur in the direction opposite the double helix twist. (inverted way of writing 8 ). More relaxed coil.
Negative supercoil→Relaxed DNA→ Positive supercoil, vise versa.
-Topoisomerases remove both positive and negative supercoils.
Topoisomerase I introduces the transient single strand breaks in DNA
Topoisomerase II introduce double-strand breaks
DNA gyrase both induce double strand breaks and supercoils.
In bacteria DNA gyrase can relax the DNA
Bacterial Chromosome
→Bacterial DNA is NEGATIVELY SUPERCOILED.
→Bacterial chromosomes are bound to few proteins that help stabilize the loops.
→Bacterial chromosome are located in the nucleoid.
Bacterial Plasmids
→Bacteria has bacterial DNA and circular plasmids.
→R factors are drug resistance genes
→Metabolic plasmids are non-essential metabolic enzymes.
→Colicinogenic factors synthesize bactericidal toxins.
→Virulence factors- synthesize disease-causing toxins.
Eukaryotic Chromosomes
→Eukaryotic DNA is organized into two types of structures: Chromatin and chromosomes
→Chromatin is long fibrous DNA or protein complexes dispersed in the nucleus.
→Chromosomes form during cell division and are larger condensed structures.
→Fluorescence In Situ Hybridization (FISH) is used for labeling DNA in cells.
DNA probes are synthesized with a fluorescent tag.
→Giemsa stain can be used to identify chromosomes in dividing cells.
→Nucleosomes are DNA complexed with histone proteins
→Chromatin fibres comes from condensed nucleosome structures.
→Heterochromatin is a further folded structure of chromatin during cell division.
→Nucleosome particle consists of DNA wrapped around a complex of histone proteins.
→Euchromatin is a loose structure of chromatin during interphase.
→Loops of chromatin fibres are stabilized by binding to cohesin proteins.
Chromatin remodelling
→Methylation of a histone tail by histone methyltransferase tightens chromatin packing.
→Acetylation by histone acetyltransferase (HAT) opens (looseen) chromatin to allow transcription.
Histone deacetylase (HDAC) reverses.
→Chromatin remodelling proteins read the histone code methylation and acetylation.
→Chromosome remodelling complexes can bind to acetylated histones and loosen the chromatin through an ATP-dependent process.
KEYPOINTS
-Centromeres
Centromeres maintain cohesions between sister chromatids during cell division
Centromeres are assembly sites for kinetochores, where microtubules attach during meiosis and mitosis.
Centromeres have a highly repetitive centromere sequence (CEN).
-Telomeres
The highly repetitive sequences can be found at the tips of chromosomes.
The telomeres protect the ends of chromosomes from falling apart during replication.
Telomeres have a highly conserved sequence of repeats in vertebrates (TTAGGG).
NUCLEUS
→The nucleus as both a storage sites for genetic information
→The nucleus is also a control centre for expression of information
NUCLEUS ENVELOP
→Nucleus is attached to a double-membraned nuclear envelope.
→Nuclear envelope has a perinuclear space 20-40nm across.
→The outer membrane of the nucleus envelop is continuous with the endoplasmic reticulum.
→Perinuclear space is continuous with the lumen of the endoplasmic reticulum.
Structure:
Nuclear envelop contains proteins that anchor the nucleus to the cytoskeleton.
Outer membrane is studded with ribosomes
Nuclear pores make the cell cytoplasm continuous with the nucleoplasm
→Nuclear Pore Complex is a large protein complex that spans the two bilayers of the nuclear envelop.
Transporter plays a role in the transport of macromolecules.
NUCLEAR PORE TRAFFIC
→Protein synthesis only occur in the cytoplasm
→Transcription occurs only in the nucleus.
→Nuclear pores drive the import and export of macromolecules across the nuclear envelop.
RAN/ IMPORTIN TRANSPORT
→Importin is a NLS binding protein that can be a transporter to shuttle proteins through the nuclear pore traffic.
→RAN is a GTPase and an exporter that shuttles the importin out of the nucleus once the the importin is unloaded.
→RAN-dependent transport also transport certain RNAs with nuclear export signals (NES) that bind exportins.
→ Nuclear Transport Factor 2 transport RAN-GDP from cytoplasm to the nucleus.
→Nuclear lamins form a nuclear scaffold to give shape to nucleus.
NUCLEOLUS
→Nucleolus is a site for rRNA synthesis
→Can be located within the nucleus that contains fibrils and granules.
Fibrils are sites of active rRNA synthesis
Granules are rRNA packaged with proteins to be exported out of the nucleus.