A bacteriophage is a virus that infects bacteria. Lambda phage is a temperate bacteriophage that has two life cycle choices: lytic and lysogenic. During lysogeny, the lambda repressor binds to the operator region (OR) on the phage DNA and represses transcription of lytic genes, allowing the phage genome to remain dormant as a prophage integrated into the bacterial chromosome.
The trp operon controls the biosynthesis of tryptophan in E. coli. It contains 5 genes that encode enzymes for tryptophan production. The operon uses attenuation to regulate expression based on tryptophan levels. When tryptophan is low, transcription proceeds through the leader sequence. When tryptophan is high, translation is rapid and a stem loop structure forms, terminating transcription. The trp operon is a repressible system, where the effector molecule allows the repressor to bind the operator and shut down expression.
The document summarizes the lac operon in E. coli, which controls the breakdown of lactose. The lac operon contains 3 genes - lacZ, lacY, and lacA - that code for enzymes involved in lactose catabolism. In the absence of lactose, a repressor protein binds to the operator region and prevents transcription. In the presence of lactose, it binds to the repressor and induces transcription of the structural genes. The lac operon demonstrates both negative control by the repressor and positive control through induction by lactose binding. Glucose also regulates the operon through catabolite repression involving cAMP levels.
Post-translational modifications (PTMs) are chemical changes that occur to proteins after translation. PTMs regulate protein activity, localization, and interactions. The main types of PTMs are phosphorylation, glycosylation, ubiquitination, and methylation. Phosphorylation involves the addition of phosphate groups and is important for cell signaling. Glycosylation adds carbohydrate groups and affects protein structure. Ubiquitination tags proteins for destruction, and methylation adds methyl groups, regulating processes like gene expression. PTMs are identified through techniques like mass spectrometry and chromatographic analysis.
Aminoglycosides like streptomycin bind to the 30S ribosomal subunit and interfere with initiation complex formation, inducing misreading of mRNA and breaking polysomes into monosomes. Chloramphenicol inhibits protein synthesis by binding reversibly to the 50S ribosomal subunit and preventing the binding of aminoacyl tRNA to the acceptor site. Tetracyclines also bind to the 30S ribosomal subunit but prevent the binding of aminoacyl tRNA to the mRNA ribosome complex. Macrolides inhibit protein synthesis by reversibly binding to the 50S ribosomal subunit and suppressing translocation of mRNA.
Protein synthesis involves three main steps - initiation, elongation, and termination. In initiation, the small and large ribosomal subunits assemble along with mRNA and tRNA to form the initiation complex. In elongation, amino acids are added one by one to the growing polypeptide chain. Termination occurs when a stop codon is reached, causing the release of the completed protein. While the overall process is similar between prokaryotes and eukaryotes, there are some key differences like the number of initiation factors and whether mRNA is polycistronic or monocistronic.
Ribosomes are organelles found in all cells that synthesize proteins. They consist of RNA and proteins and exist as two subunits - a smaller 30S subunit in prokaryotes and 40S in eukaryotes, and a larger 50S subunit in prokaryotes and 60S in eukaryotes. Ribosomes translate mRNA into proteins through initiation, elongation, and termination steps. Errors in ribosome functioning can lead to improper protein folding and diseases.
This document discusses genetic code, tRNA, and translation. It provides definitions of key terms like codon, anticodon, wobble hypothesis. It describes the structure and function of tRNA, including how it is charged with specific amino acids by aminoacyl tRNA synthetases. The document also discusses characteristics of the genetic code, including that it is degenerate, uses triplet codons, and has start and stop signals. It provides information on ribosomes, including their composition in prokaryotes and eukaryotes. In summary, the document provides an overview of the mechanisms and key components involved in translating genetic code into proteins.
Mutation is a change in genetic material that can be caused by errors during DNA replication or DNA repair. There are several types of mutations including point mutations, insertions, deletions, and chromosomal mutations. Point mutations include transitions, transversions, missense mutations, and nonsense mutations. Insertions and deletions can disrupt the genetic code. Spontaneous mutations arise naturally while induced mutations are caused by mutagens like radiation, chemicals, or viruses. Mutations can be germline or somatic and can have different effects on protein function and the phenotype. The document provides examples of specific mutations and their effects.
Telomeres are repetitive DNA sequences at the ends of chromosomes that protect them from degradation. Telomeres naturally shorten each time a cell divides until they reach a critical shortness that causes cell senescence. Telomerase is an enzyme that adds telomere repeats to chromosome ends and counteracts shortening. It is active in 90% of cancer cells, allowing unlimited cell division by maintaining telomere length, but is not generally active in most adult somatic cells.
This document discusses DNA replication and the central dogma. It covers the basic requirements for DNA replication including substrates, templates, enzymes, and primers. The stages of replication - initiation, elongation, and termination - are described. Key aspects of the replication process are explained, such as semi-conservative mechanism, unwinding of DNA, formation of replication forks, and bidirectional replication. Differences between prokaryotic and eukaryotic DNA replication are highlighted. Finally, various inhibitors of DNA replication are listed.
RNA differs from DNA in several key ways. RNA is typically single-stranded, contains ribose sugar instead of deoxyribose, and contains uracil instead of thymine. There are multiple types of RNA that serve different cellular functions, including messenger RNA (mRNA), transfer RNA (tRNA), and ribosomal RNA (rRNA). mRNA carries coding information from DNA to the ribosome for protein synthesis. tRNA transfers amino acids to the ribosome during protein assembly according to the mRNA codon sequence. rRNA is a core component of ribosomes and facilitates protein translation.
Transcriptional regulatory elements such as promoters, enhancers, silencers, and insulators help control gene expression. Promoters initiate transcription and contain core and proximal elements. Enhancers can activate transcription from farther distances by binding activator proteins. Silencers negatively regulate genes by binding repressor proteins. Insulators block interactions between genes to prevent neighboring transcriptional effects. These cis-acting elements help precisely regulate protein levels through transcriptional mechanisms.
Ribozymes are RNA molecules that act as enzymes and catalyze biochemical reactions. They were first discovered in 1982 by Thomas Czech and Sidney Altman, who later won the Nobel Prize in Chemistry for their discovery. Ribozymes increase the rate and specificity of reactions like phosphodiester bond cleavage and peptide bond synthesis. Common types of ribozymes include self-splicing introns, RNase P, hammerhead ribozymes, and hairpin ribozymes. Artificial ribozymes can also be synthesized in the laboratory by mutating natural ribozymes.
Rifampicin binds to the beta subunit of prokaryotic RNA polymerase, inhibiting prokaryotic transcription initiation. It selectively binds bacterial RNA polymerase without affecting eukaryotic polymerases. This allows rifampicin to be an effective treatment for bacterial infections like tuberculosis and leprosy. Alpha amanitin from death cap mushrooms potently inhibits RNA polymerase II during both transcription initiation and elongation, potentially causing death in 10 days from just one mushroom due to failure of gene expression.
Eukaryotic pre-mRNA undergoes processing in the nucleus before being exported to the cytoplasm for protein synthesis. This involves adding a 5' cap and poly-A tail to increase stability and facilitate export. Introns are also spliced out by the spliceosome, a complex of small nuclear RNAs and proteins that cuts out introns and joins exons to form mature mRNA. Capping occurs at the 5' end shortly after transcription, while polyadenylation adds around 200 adenine nucleotides to the 3' end. Splicing removes intervening intron sequences by cutting and religating exons. These processing steps produce translation-competent mRNA from initial pre-mRNA transcripts.
The document summarizes transcription in prokaryotes. It discusses the key components including the template strand, coding strand, and RNA polymerase. RNA polymerase is made up of multiple subunits and recognizes promoter sequences to initiate transcription. The process of transcription involves three phases - initiation when RNA polymerase binds to the promoter, elongation as the RNA strand continuously grows, and termination when RNA polymerase stops synthesis.
DNA is a double-helix molecule that carries genetic instructions. It is composed of two strands called polynucleotides made up of nucleotides, each containing a nucleobase (A, T, C, or G), sugar, and phosphate. The strands are stabilized by hydrogen bonds between nucleotides and base stacking. DNA can be denatured by heat, pH extremes, or chemicals, breaking the hydrogen bonds and separating the strands. Denaturation temperature depends on factors like composition, length, and environment. Renaturation occurs when strands reconnect under appropriate conditions.
DNA's double helical structure is stabilized by several weak forces that collectively provide strong stabilization. Hydrogen bonding between complementary base pairs provides some stability, while base stacking interactions between the hydrophobic bases, including hydrophobic and van der Waals forces, provide additional stability by burying the bases in the interior. Ionic interactions between the negatively charged phosphate backbone and positive ions like magnesium also contribute to stability. Though each individual interaction is weak, the collective effects of all of these forces interacting along the entire DNA molecule strongly stabilize its double helical structure.
Nucleic acids like DNA and RNA contain the genetic information of living organisms. DNA specifically stores and carries genetic information in the form of genes. It has a double helix structure with two strands coiled around each other. Each strand is made up of repeating nucleotide units containing a phosphate, sugar (deoxyribose in DNA), and one of four nitrogenous bases (A, T, C, G). The bases on each strand bond with each other through hydrogen bonds - A pairs with T and C pairs with G. This discovery of DNA's double helix structure was made in 1953 by James Watson and Francis Crick based on experimental evidence from scientists like Rosalind Franklin, Maurice Wilkins, and Erwin Charg
1. Plants have internal mechanisms for tolerating variations in external environments like water deficit, cold, and heat stress.
2. Engineering stress tolerance focuses on producing osmoprotectants like glycine betaine and sorbitol to reduce osmotic stress from water deficit. Glycine betaine is produced through pathways using enzymes like choline monooxygenase.
3. Salt tolerance has been engineered by transforming plants with genes for vacuolar antiport proteins like NHX1 to transport sodium ions out of cells.
Dr.S.KARTHIKUMAR
Associate Professor
Department of Biotechnology
Kamaraj College of Engineering and Technology, K.Vellakulam-625701, TN, India
Email: skarthikumar@gmail.com
Dr.S.KARTHIKUMAR
Associate Professor
Department of Biotechnology
Kamaraj College of Engineering and Technology, K.Vellakulam-625701, TN, India
Email: skarthikumar@gmail.com
Dr.S.KARTHIKUMAR
Associate Professor
Department of Biotechnology
Kamaraj College of Engineering and Technology, K.Vellakulam-625701, TN, India
Email: skarthikumar@gmail.com
Dr.S.KARTHIKUMAR
Associate Professor
Department of Biotechnology
Kamaraj College of Engineering and Technology, K.Vellakulam-625701, TN, India
Email: skarthikumar@gmail.com
Dr.S.KARTHIKUMAR
Associate Professor
Department of Biotechnology
Kamaraj College of Engineering and Technology, K.Vellakulam-625701, TN, India
Email: skarthikumar@gmail.com
Dr.S.KARTHIKUMAR
Associate Professor
Department of Biotechnology
Kamaraj College of Engineering and Technology, K.Vellakulam-625701, TN, India
Email: skarthikumar@gmail.com
Dr.S.KARTHIKUMAR
Associate Professor
Department of Biotechnology
Kamaraj College of Engineering and Technology, K.Vellakulam-625701, TN, India
Email: skarthikumar@gmail.com
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Mutation is a change in genetic material that can be caused by errors during DNA replication or DNA repair. There are several types of mutations including point mutations, insertions, deletions, and chromosomal mutations. Point mutations include transitions, transversions, missense mutations, and nonsense mutations. Insertions and deletions can disrupt the genetic code. Spontaneous mutations arise naturally while induced mutations are caused by mutagens like radiation, chemicals, or viruses. Mutations can be germline or somatic and can have different effects on protein function and the phenotype. The document provides examples of specific mutations and their effects.
Telomeres are repetitive DNA sequences at the ends of chromosomes that protect them from degradation. Telomeres naturally shorten each time a cell divides until they reach a critical shortness that causes cell senescence. Telomerase is an enzyme that adds telomere repeats to chromosome ends and counteracts shortening. It is active in 90% of cancer cells, allowing unlimited cell division by maintaining telomere length, but is not generally active in most adult somatic cells.
This document discusses DNA replication and the central dogma. It covers the basic requirements for DNA replication including substrates, templates, enzymes, and primers. The stages of replication - initiation, elongation, and termination - are described. Key aspects of the replication process are explained, such as semi-conservative mechanism, unwinding of DNA, formation of replication forks, and bidirectional replication. Differences between prokaryotic and eukaryotic DNA replication are highlighted. Finally, various inhibitors of DNA replication are listed.
RNA differs from DNA in several key ways. RNA is typically single-stranded, contains ribose sugar instead of deoxyribose, and contains uracil instead of thymine. There are multiple types of RNA that serve different cellular functions, including messenger RNA (mRNA), transfer RNA (tRNA), and ribosomal RNA (rRNA). mRNA carries coding information from DNA to the ribosome for protein synthesis. tRNA transfers amino acids to the ribosome during protein assembly according to the mRNA codon sequence. rRNA is a core component of ribosomes and facilitates protein translation.
Transcriptional regulatory elements such as promoters, enhancers, silencers, and insulators help control gene expression. Promoters initiate transcription and contain core and proximal elements. Enhancers can activate transcription from farther distances by binding activator proteins. Silencers negatively regulate genes by binding repressor proteins. Insulators block interactions between genes to prevent neighboring transcriptional effects. These cis-acting elements help precisely regulate protein levels through transcriptional mechanisms.
Ribozymes are RNA molecules that act as enzymes and catalyze biochemical reactions. They were first discovered in 1982 by Thomas Czech and Sidney Altman, who later won the Nobel Prize in Chemistry for their discovery. Ribozymes increase the rate and specificity of reactions like phosphodiester bond cleavage and peptide bond synthesis. Common types of ribozymes include self-splicing introns, RNase P, hammerhead ribozymes, and hairpin ribozymes. Artificial ribozymes can also be synthesized in the laboratory by mutating natural ribozymes.
Rifampicin binds to the beta subunit of prokaryotic RNA polymerase, inhibiting prokaryotic transcription initiation. It selectively binds bacterial RNA polymerase without affecting eukaryotic polymerases. This allows rifampicin to be an effective treatment for bacterial infections like tuberculosis and leprosy. Alpha amanitin from death cap mushrooms potently inhibits RNA polymerase II during both transcription initiation and elongation, potentially causing death in 10 days from just one mushroom due to failure of gene expression.
Eukaryotic pre-mRNA undergoes processing in the nucleus before being exported to the cytoplasm for protein synthesis. This involves adding a 5' cap and poly-A tail to increase stability and facilitate export. Introns are also spliced out by the spliceosome, a complex of small nuclear RNAs and proteins that cuts out introns and joins exons to form mature mRNA. Capping occurs at the 5' end shortly after transcription, while polyadenylation adds around 200 adenine nucleotides to the 3' end. Splicing removes intervening intron sequences by cutting and religating exons. These processing steps produce translation-competent mRNA from initial pre-mRNA transcripts.
The document summarizes transcription in prokaryotes. It discusses the key components including the template strand, coding strand, and RNA polymerase. RNA polymerase is made up of multiple subunits and recognizes promoter sequences to initiate transcription. The process of transcription involves three phases - initiation when RNA polymerase binds to the promoter, elongation as the RNA strand continuously grows, and termination when RNA polymerase stops synthesis.
DNA is a double-helix molecule that carries genetic instructions. It is composed of two strands called polynucleotides made up of nucleotides, each containing a nucleobase (A, T, C, or G), sugar, and phosphate. The strands are stabilized by hydrogen bonds between nucleotides and base stacking. DNA can be denatured by heat, pH extremes, or chemicals, breaking the hydrogen bonds and separating the strands. Denaturation temperature depends on factors like composition, length, and environment. Renaturation occurs when strands reconnect under appropriate conditions.
DNA's double helical structure is stabilized by several weak forces that collectively provide strong stabilization. Hydrogen bonding between complementary base pairs provides some stability, while base stacking interactions between the hydrophobic bases, including hydrophobic and van der Waals forces, provide additional stability by burying the bases in the interior. Ionic interactions between the negatively charged phosphate backbone and positive ions like magnesium also contribute to stability. Though each individual interaction is weak, the collective effects of all of these forces interacting along the entire DNA molecule strongly stabilize its double helical structure.
Nucleic acids like DNA and RNA contain the genetic information of living organisms. DNA specifically stores and carries genetic information in the form of genes. It has a double helix structure with two strands coiled around each other. Each strand is made up of repeating nucleotide units containing a phosphate, sugar (deoxyribose in DNA), and one of four nitrogenous bases (A, T, C, G). The bases on each strand bond with each other through hydrogen bonds - A pairs with T and C pairs with G. This discovery of DNA's double helix structure was made in 1953 by James Watson and Francis Crick based on experimental evidence from scientists like Rosalind Franklin, Maurice Wilkins, and Erwin Charg
1. Plants have internal mechanisms for tolerating variations in external environments like water deficit, cold, and heat stress.
2. Engineering stress tolerance focuses on producing osmoprotectants like glycine betaine and sorbitol to reduce osmotic stress from water deficit. Glycine betaine is produced through pathways using enzymes like choline monooxygenase.
3. Salt tolerance has been engineered by transforming plants with genes for vacuolar antiport proteins like NHX1 to transport sodium ions out of cells.
Dr.S.KARTHIKUMAR
Associate Professor
Department of Biotechnology
Kamaraj College of Engineering and Technology, K.Vellakulam-625701, TN, India
Email: skarthikumar@gmail.com
Dr.S.KARTHIKUMAR
Associate Professor
Department of Biotechnology
Kamaraj College of Engineering and Technology, K.Vellakulam-625701, TN, India
Email: skarthikumar@gmail.com
Dr.S.KARTHIKUMAR
Associate Professor
Department of Biotechnology
Kamaraj College of Engineering and Technology, K.Vellakulam-625701, TN, India
Email: skarthikumar@gmail.com
Dr.S.KARTHIKUMAR
Associate Professor
Department of Biotechnology
Kamaraj College of Engineering and Technology, K.Vellakulam-625701, TN, India
Email: skarthikumar@gmail.com
Dr.S.KARTHIKUMAR
Associate Professor
Department of Biotechnology
Kamaraj College of Engineering and Technology, K.Vellakulam-625701, TN, India
Email: skarthikumar@gmail.com
Dr.S.KARTHIKUMAR
Associate Professor
Department of Biotechnology
Kamaraj College of Engineering and Technology, K.Vellakulam-625701, TN, India
Email: skarthikumar@gmail.com
Dr.S.KARTHIKUMAR
Associate Professor
Department of Biotechnology
Kamaraj College of Engineering and Technology, K.Vellakulam-625701, TN, India
Email: skarthikumar@gmail.com
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