Introduction
Protein synthesis
Synthesis of secretory proteins on membrane-bound ribosomes
Processing of newly synthesized proteins in the ER
Synthesis of integral membrane protein on membrane bound ribosomes
Maintenance of membrane asymmetry
Conclusion
Reference
Protein targeting or protein sorting is the mechanism by which a cell transports to the appropriate positions in the cell or outside of it. Both in prokaryotes and eukaryotes, newly synthesized proteins must be delivered to a specific sub-cellular location or exported from the cell for correct activity. This phenomenon is called protein targeting. Protein targeting is necessary for proteins that are destined to work outside the cytoplasm.This delivery process is carried out based on information contained in the protein itself. Correct sorting is crucial for the cell; errors can lead to diseases. In 1970, Günter Blobel conducted experiments on the translocation of proteins across membranes. He was awarded the 1999 Nobel Prize for his findings. He discovered that many proteins have a signal sequence, that is, a short amino acid sequence at one end that functions like a postal code for the target organelle.
In this slideshare, we know about the DNA supercoiling. How does it forms, size of DNA in a human body. How the chromosomes are formed. Useful enzymes that regulate the coiling of DNA. Relaxing stage of DNA which is circular form the left handed and right handed DNA coiling. Mostly in our body left handed coiling DNA are found. Importance of coiling their function and little bit of the structure of Supercoiling.
Protein targeting or protein sorting is the biological mechanism by which proteins are transported to their appropriate destinations in the cell or outside it. Proteins can be targeted to the inner space of an organelle, different intracellular membranes, plasma membrane, or to exterior of the cell via secretion.
Protein targeting or protein sorting is the mechanism by which a cell transports to the appropriate positions in the cell or outside of it. Both in prokaryotes and eukaryotes, newly synthesized proteins must be delivered to a specific sub-cellular location or exported from the cell for correct activity. This phenomenon is called protein targeting. Protein targeting is necessary for proteins that are destined to work outside the cytoplasm.This delivery process is carried out based on information contained in the protein itself. Correct sorting is crucial for the cell; errors can lead to diseases. In 1970, Günter Blobel conducted experiments on the translocation of proteins across membranes. He was awarded the 1999 Nobel Prize for his findings. He discovered that many proteins have a signal sequence, that is, a short amino acid sequence at one end that functions like a postal code for the target organelle.
In this slideshare, we know about the DNA supercoiling. How does it forms, size of DNA in a human body. How the chromosomes are formed. Useful enzymes that regulate the coiling of DNA. Relaxing stage of DNA which is circular form the left handed and right handed DNA coiling. Mostly in our body left handed coiling DNA are found. Importance of coiling their function and little bit of the structure of Supercoiling.
Protein targeting or protein sorting is the biological mechanism by which proteins are transported to their appropriate destinations in the cell or outside it. Proteins can be targeted to the inner space of an organelle, different intracellular membranes, plasma membrane, or to exterior of the cell via secretion.
CBCS 4TH SEM ,
CHARGING, STRUCTURE AND FUNCTION OF tRNA,
AMINOACYL RNA SYNTHETASE(ASR) PROOFREADING AND EDITING
https://www.youtube.com/watch?v=YzOVMWYLiCE
Dna supercoiling and role of topoisomerasesYashwanth B S
supercoiling is one of the important process to condenses the huge amount of DNA to fit inside the histone and its also plays a role during the replication ,transcription etc..,these activities is carried out by an enzyme called topoisomerases.
It is the process of synthesis of protein by encoding information on mRNA.
Protein synthesis requires mRNA, tRNA, aminoacids, ribosome and enzyme aminoacyl tRNA synthase
Proteins destined for secretion, integration in the plasma membrane, or inclusion in lysosomes generally share pathway that begins in the endoplasmic reticulum. Proteins destined for mitochondria, chloroplasts, or the nucleus use three separate mechanisms. And proteins destined for the cytosol simply remain where they are synthesized.
CBCS 4TH SEM ,
CHARGING, STRUCTURE AND FUNCTION OF tRNA,
AMINOACYL RNA SYNTHETASE(ASR) PROOFREADING AND EDITING
https://www.youtube.com/watch?v=YzOVMWYLiCE
Dna supercoiling and role of topoisomerasesYashwanth B S
supercoiling is one of the important process to condenses the huge amount of DNA to fit inside the histone and its also plays a role during the replication ,transcription etc..,these activities is carried out by an enzyme called topoisomerases.
It is the process of synthesis of protein by encoding information on mRNA.
Protein synthesis requires mRNA, tRNA, aminoacids, ribosome and enzyme aminoacyl tRNA synthase
Proteins destined for secretion, integration in the plasma membrane, or inclusion in lysosomes generally share pathway that begins in the endoplasmic reticulum. Proteins destined for mitochondria, chloroplasts, or the nucleus use three separate mechanisms. And proteins destined for the cytosol simply remain where they are synthesized.
Proteins destined for secretion, integration in the plasma membrane, or inclusion in lysosomes generally share pathway that begins in the endoplasmic reticulum. Proteins destined for mitochondria, chloroplasts, or the nucleus use three separate mechanisms. And proteins destined for the cytosol simply remain where they are synthesized.
Describe the role signal sequences play in protein localization. NES.pdffippsximenaal85949
Describe the role signal sequences play in protein localization. NES, NJS, Stop start, ER signal
sequences Describe the process of events involved in ligand production to exocytosis.
PowerPointslide 6 plus written details Post transcriptional modifications. Discuss 5\'capping,
splicing, poly A tail Describe three different mechanisms of signal termination Inhibitors -
extracellular, receptor inhibitors, internalization phosphorylation/dephosphorylation Give an
account of the role vesicle tethering plays in endocytosis. SNARES V and T, Rab effectors,
tethering docking fusion Protein glycosylation, discuss, its importance and the process of
glycosylation Occurs in ER, modified in Golgi, etc... Autocrine, paracrine and endocrine.
Discuss the differences between these signaling mechanisms. Write an account how signaling
can be terminated at the level of receptors Different cells can react differently to the same signal.
Discuss Example acetylcholine Outline the process of plasma membrane receptor production to
its final destination Two major populations of ribosome exist in our cells. Discuss
Solution
Ques-1:
The role of signal seqeunecs in protein localization:
ER signal sequences and stop-start:
Signal peptidase normally localized in the “endoplasmic reticulum” of eukaryotic cell. These
serine proteases digest the “nascent secretory polypeptides” after translation & post & co-
translational modifications. These signal peptidase enzymes are going to cleave signal peptides
of membrane proteins at their N-terminals.
Signal sequence of \"6 to 10 amino acid length\" normally cleaved by signal peptidases during or
after completion of translocation from ribosome & before entering into the endoplasmic
reticulum
Cotranslational translocation is mediated by signal recognition particle (SRP) & it is a 11S
ribonucleoprotien essential for translocation of nascent polypeptide to the “ER lumen”. This SRP
is formed of a nucleoprotein with 7S RNA, 11S & combines with several proteins to form the
eukaryotic signal recognition particle. The nascent polypeptide is emerged from the ribosomes,
followed by “recognition of signal sequence & bound by signal recognition particle(SRP), a
hydrophobic residue with 6 polypeptides 7SL RNA.
Therefore, when this SRP sequence exits from the ribosome, the nascent polypeptide stops being
translocated into the ER lumen. Signal recognition particle has bound by a signal sequence and
flowed by slow protein synthesis in the translation. This SRP further is going to bind to the
location near by endoplasmic reticulum followed by release of signal recognition particle but the
growing polypeptide is in the form of protein-ribosome complex that is at the exact location for
further protein translocation through Golgi-vesicle translocation channel.
The nuclear localization signal sequence (NLS) is mainly associated with “tags” in which amino
acids or proteins are imported into the nucleus using Ran-GTPases activity by nuclear transport.
So .
Introduction
History
Tumor suppressor gene- pRB
- RB gene
- Role of RB in regulation of cell cycle
- Tumor associated with RB gene mutation
Tumor suppressor gene- p53
- What is p53 gene?
- Function of p53 gene
- How it regulates cell cycle
- What happen if p53 gene inactivated
- Cancer associated with p53 mutation
- Conclusion
- References
Introduction
Definition
History
Two hit hypothesis
Functions
Mutation in tumor suppressor genes
What is mutation
Inherited mutation of TSGs
Acquired mutation of TSGs
What is Oncogenes?
TSGs and Oncogenes : Brakes and accelerators
Stop and go signal
Examples of TSGs:
RB-The retinoblastoma gene
P53 protein
TSGs &cell suicide
Conclusion
References
Introduction
Definition
Factors required for Translation
Formation of aminoacyl t-RNA
1)Activation of amino acid
2) Transfer of amino acid to t-RNA
Translation involves following steps:-
1)Initiation
2)Elongation
3)Termination
Conclusion
Reference
Introduction
Definition
History
central dogma
Major components
mRNA,tRNA,rRNA
Energy source
Amino acids
Protien factor
Enzymes
Inorganic ions
Step involves in translation:
Aminoacylation of tRNA
Initiation
Elongation
termination
Importance of translation
Conclusion
Reference
Introduction
Protein modifications
Folding
Chaperon mediated
Enzymatic
Cleavage
Addition of functional groups
Chemical groups
Hydrophobic groups
Proteolysis
Conclusion
Reference
INTRODUCTION
HISTORY
WHAT IS TRANSCRIPTION
PROKARYOTIC TRANSCRIPTION
STEPS OF TRANSCRIPTION
HOW TRANSCRIPTION OCCURS
PROCESS OF TRANSCRIPTION
Initiation
Elongation
Termination
CONCLUSION
REFRENCES
Enzyme Kinetics and thermodynamic analysisKAUSHAL SAHU
Introduction
Kinetics and thermodynamicSG
Thermodynamic in enzymatic reactions
balanced equations in chemical reactions
changes in free energy determine the direction & equilibrium state of chemical reactions
the rates of reactions
Factors effecting enzymatic activity
(i) Enzyme concentration.
(ii) Substrate concentration.
(iii)Temperature
(iv) pH.
(v) Activators.
(vi)Inhibitors
Michaelis-menten equation
CONCLUSIONS
REFERENECES
Recepter mediated endocytosis by kk ashuKAUSHAL SAHU
INTRODUCTION
DEFINITION OF RECEPTOR MEDIATED ENDOCYTOSIS
WHAT TYPE OF LIGANDS ENTER BY RME?
FORMATION OF CLATHRIN-COATED VESICLES
TRISKELIONS
ROLE OF DYNAMIN IN THE FORMATION OF CLATHRIN-COATED VESICLES
ROLE OF PHOSPHOLIPIDS IN THE FORMATION OF COATED VESICLES
ENDOCYTIC PATHWAY
LDLs AND CHOLESTROL METABOLISM
CONCLUSION
REFERENCES
The delivery of newly synthesized protein to their proper cellular destination, usually referred to as protein targeting or sorting.
The mode of protein transport depends chiefly on the location in the cell cytoplasm of the polysomes involved in protein synthesis.
There are two modes of protein sorting:-
1) Co - translational Transportation.
2) Post - translational Transportation.
Prokaryotic translation machinery by kk KAUSHAL SAHU
Introduction
Definition
Factors required for Translation
Formation of aminoacyl t-RNA
1)Activation of amino acid
2) Transfer of amino acid to t-RNA
Translation involves following steps:-
1)Initiation
2)Elongation
3)Termination
Conclusion
Reference
INTRODUCTION.
HISTORY.
PROCESS OF TRANSCRIPTION.
STAGES OF TRANSCRIPTION.
ENZYME INVOLVES IN TRANSCRIPTION.
TERMINATION.
PROKARYOTES.
Transcription terminators.
EUKARYOTES.
Two models for termination.
CONCLUSION.
REFERENCES.
Nutraceutical market, scope and growth: Herbal drug technologyLokesh Patil
As consumer awareness of health and wellness rises, the nutraceutical market—which includes goods like functional meals, drinks, and dietary supplements that provide health advantages beyond basic nutrition—is growing significantly. As healthcare expenses rise, the population ages, and people want natural and preventative health solutions more and more, this industry is increasing quickly. Further driving market expansion are product formulation innovations and the use of cutting-edge technology for customized nutrition. With its worldwide reach, the nutraceutical industry is expected to keep growing and provide significant chances for research and investment in a number of categories, including vitamins, minerals, probiotics, and herbal supplements.
Richard's entangled aventures in wonderlandRichard Gill
Since the loophole-free Bell experiments of 2020 and the Nobel prizes in physics of 2022, critics of Bell's work have retreated to the fortress of super-determinism. Now, super-determinism is a derogatory word - it just means "determinism". Palmer, Hance and Hossenfelder argue that quantum mechanics and determinism are not incompatible, using a sophisticated mathematical construction based on a subtle thinning of allowed states and measurements in quantum mechanics, such that what is left appears to make Bell's argument fail, without altering the empirical predictions of quantum mechanics. I think however that it is a smoke screen, and the slogan "lost in math" comes to my mind. I will discuss some other recent disproofs of Bell's theorem using the language of causality based on causal graphs. Causal thinking is also central to law and justice. I will mention surprising connections to my work on serial killer nurse cases, in particular the Dutch case of Lucia de Berk and the current UK case of Lucy Letby.
Seminar of U.V. Spectroscopy by SAMIR PANDASAMIR PANDA
Spectroscopy is a branch of science dealing the study of interaction of electromagnetic radiation with matter.
Ultraviolet-visible spectroscopy refers to absorption spectroscopy or reflect spectroscopy in the UV-VIS spectral region.
Ultraviolet-visible spectroscopy is an analytical method that can measure the amount of light received by the analyte.
Professional air quality monitoring systems provide immediate, on-site data for analysis, compliance, and decision-making.
Monitor common gases, weather parameters, particulates.
Richard's aventures in two entangled wonderlandsRichard Gill
Since the loophole-free Bell experiments of 2020 and the Nobel prizes in physics of 2022, critics of Bell's work have retreated to the fortress of super-determinism. Now, super-determinism is a derogatory word - it just means "determinism". Palmer, Hance and Hossenfelder argue that quantum mechanics and determinism are not incompatible, using a sophisticated mathematical construction based on a subtle thinning of allowed states and measurements in quantum mechanics, such that what is left appears to make Bell's argument fail, without altering the empirical predictions of quantum mechanics. I think however that it is a smoke screen, and the slogan "lost in math" comes to my mind. I will discuss some other recent disproofs of Bell's theorem using the language of causality based on causal graphs. Causal thinking is also central to law and justice. I will mention surprising connections to my work on serial killer nurse cases, in particular the Dutch case of Lucia de Berk and the current UK case of Lucy Letby.
Earliest Galaxies in the JADES Origins Field: Luminosity Function and Cosmic ...Sérgio Sacani
We characterize the earliest galaxy population in the JADES Origins Field (JOF), the deepest
imaging field observed with JWST. We make use of the ancillary Hubble optical images (5 filters
spanning 0.4−0.9µm) and novel JWST images with 14 filters spanning 0.8−5µm, including 7 mediumband filters, and reaching total exposure times of up to 46 hours per filter. We combine all our data
at > 2.3µm to construct an ultradeep image, reaching as deep as ≈ 31.4 AB mag in the stack and
30.3-31.0 AB mag (5σ, r = 0.1” circular aperture) in individual filters. We measure photometric
redshifts and use robust selection criteria to identify a sample of eight galaxy candidates at redshifts
z = 11.5 − 15. These objects show compact half-light radii of R1/2 ∼ 50 − 200pc, stellar masses of
M⋆ ∼ 107−108M⊙, and star-formation rates of SFR ∼ 0.1−1 M⊙ yr−1
. Our search finds no candidates
at 15 < z < 20, placing upper limits at these redshifts. We develop a forward modeling approach to
infer the properties of the evolving luminosity function without binning in redshift or luminosity that
marginalizes over the photometric redshift uncertainty of our candidate galaxies and incorporates the
impact of non-detections. We find a z = 12 luminosity function in good agreement with prior results,
and that the luminosity function normalization and UV luminosity density decline by a factor of ∼ 2.5
from z = 12 to z = 14. We discuss the possible implications of our results in the context of theoretical
models for evolution of the dark matter halo mass function.
Introduction:
RNA interference (RNAi) or Post-Transcriptional Gene Silencing (PTGS) is an important biological process for modulating eukaryotic gene expression.
It is highly conserved process of posttranscriptional gene silencing by which double stranded RNA (dsRNA) causes sequence-specific degradation of mRNA sequences.
dsRNA-induced gene silencing (RNAi) is reported in a wide range of eukaryotes ranging from worms, insects, mammals and plants.
This process mediates resistance to both endogenous parasitic and exogenous pathogenic nucleic acids, and regulates the expression of protein-coding genes.
What are small ncRNAs?
micro RNA (miRNA)
short interfering RNA (siRNA)
Properties of small non-coding RNA:
Involved in silencing mRNA transcripts.
Called “small” because they are usually only about 21-24 nucleotides long.
Synthesized by first cutting up longer precursor sequences (like the 61nt one that Lee discovered).
Silence an mRNA by base pairing with some sequence on the mRNA.
Discovery of siRNA?
The first small RNA:
In 1993 Rosalind Lee (Victor Ambros lab) was studying a non- coding gene in C. elegans, lin-4, that was involved in silencing of another gene, lin-14, at the appropriate time in the
development of the worm C. elegans.
Two small transcripts of lin-4 (22nt and 61nt) were found to be complementary to a sequence in the 3' UTR of lin-14.
Because lin-4 encoded no protein, she deduced that it must be these transcripts that are causing the silencing by RNA-RNA interactions.
Types of RNAi ( non coding RNA)
MiRNA
Length (23-25 nt)
Trans acting
Binds with target MRNA in mismatch
Translation inhibition
Si RNA
Length 21 nt.
Cis acting
Bind with target Mrna in perfect complementary sequence
Piwi-RNA
Length ; 25 to 36 nt.
Expressed in Germ Cells
Regulates trnasposomes activity
MECHANISM OF RNAI:
First the double-stranded RNA teams up with a protein complex named Dicer, which cuts the long RNA into short pieces.
Then another protein complex called RISC (RNA-induced silencing complex) discards one of the two RNA strands.
The RISC-docked, single-stranded RNA then pairs with the homologous mRNA and destroys it.
THE RISC COMPLEX:
RISC is large(>500kD) RNA multi- protein Binding complex which triggers MRNA degradation in response to MRNA
Unwinding of double stranded Si RNA by ATP independent Helicase
Active component of RISC is Ago proteins( ENDONUCLEASE) which cleave target MRNA.
DICER: endonuclease (RNase Family III)
Argonaute: Central Component of the RNA-Induced Silencing Complex (RISC)
One strand of the dsRNA produced by Dicer is retained in the RISC complex in association with Argonaute
ARGONAUTE PROTEIN :
1.PAZ(PIWI/Argonaute/ Zwille)- Recognition of target MRNA
2.PIWI (p-element induced wimpy Testis)- breaks Phosphodiester bond of mRNA.)RNAse H activity.
MiRNA:
The Double-stranded RNAs are naturally produced in eukaryotic cells during development, and they have a key role in regulating gene expression .
1. By
KAUSHAL KUMAR SAHU
Assistant Professor (Ad Hoc)
Department of Biotechnology
Govt. Digvijay Autonomous P. G. College
Raj-Nandgaon ( C. G. )
2. Introduction
Protein synthesis
Synthesis of secretory proteins on membrane-bound ribosomes
Processing of newly synthesized proteins in the ER
Synthesis of integral membrane protein on membrane bound
ribosomes
Maintenance of membrane asymmetry
Conclusion
Reference
3. The rough ER is the starting point of the
biosynthetic pathway: it is the site of synthesis of
the proteins, carbohydrate chains, and
phospholipids.
Certain polypeptides are synthesized on ribosomes
attached to the cytosolic surface of the RER
membranes.
Other polypeptides are synthesized on “free”
ribosomes.
4. It includes: transcription and translation.
Transcription- In transcription an mRNA chain is
generated, with one strand of the DNA double helix
in the genome as template.
Translation- The synthesis of proteins is
known as translation. In translation, mRNA is
decoded to produce a specific polypeptide. This
uses an mRNA sequence as a template to guide
the synthesis of a chain of amino acids that form a
protein.
5. •Ribosomes synthesizing nascent proteins in the secretory pathway are
directed to the RER.
•After translation is completed on the ER, these proteins can move via
transport vesicles to the Golgi complex.
• Further sorting delivers proteins either to the plasma membrane or to
the lysosomes.
6. Polypeptides synthesized on membrane bound ribosomes
contain a signal sequence—which includes a stretch of 6–15
hydrophobic amino acid residues—that targets the nascent
polypeptide to the ER membrane.
As it emerges from the ribosome, the hydrophobic signal
sequence is recognized by a signal recognition
particle(SRP).
The SRP binds to both the signal sequence on the nascent
polypeptide and the ribosome.
Binding to the ER occurs through at least two distinct
interactions: one between the SRP and the SRP receptor,
and the other between the ribosome and the translocon
7. •Once the SRP-ribosome-nascent chain complex binds to the ER membrane,
the SRP is released from its ER receptor, the ribosome becomes attached to
the cytosolic end of the translocon, and the signal sequence on the nascent
polypeptide is inserted into the narrow aqueous channel of the translocon.
• The growing polypeptide is then translocated through the hydrophobic pore
ring and into the ER lumen.
8. The N-terminal portion containing the signal peptide is removed from
most nascent polypeptides by a proteolytic enzyme, the signal
peptidase.
Carbohydrates are added to the nascent protein by the enzyme
oligosaccharyltransferase.
The RER lumen is packed with molecular chaperones that recognize
and bind to unfolded or misfolded proteins and give them the
opportunity to attain their correct (native) three-dimensional structure .
The ER lumen also contains a number of protein-processing
enzymes,such as protein disulfide isomerase (PDI ).
The formation (and rearrangement) of disulfide bonds is catalyzed by
PDI.
9. Integral membrane proteins are also synthesized on membrane-bound
ribosomes of the ER.
Integral proteins contain one or more hydrophobic transmembrane segments
that block further movement of protein into the ER lumen.
These segments,called stop-transfer sequences,typically include at least
15 continous hydrophobic or uncharged amino acid residues that allow
stable integration into the lipid bilayer of the ER membrane.
During the synthesis of membrane proteins, the inner lining of the
translocon is thought to orient the nascent polypeptide so that the more
positive end faces the cytosol.
As a polypeptide passes through the translocon, it is proposed that this
lateral “gate” in the channel continually opens and closes, which gives each
segment of the nascent polypeptide an opportunity to partition itself
according to its solubility properties into either the aqueous compartment
within the translocon channel or the surrounding hydrophobic core of the lipid
bilayer.
10. •The nascent polypeptide enters the translocon just as if it were a secretory
protein (step 1-3).
•However, the entry of the hydrophobic stop-transfer sequence into the pore
blocks further translocation of nascent polypeptide through the channel(step 4).
•The ribosomes remain attached to the translocon, but is “tipped” so as to allow
the remaining portion of polypeptide ( the C-terminal portion) to be synthesized
in the cytosol. (step 5).
•Because ribosome is no longer tightly attached to the cytosolic end of the
translocon, a protein must bind on the luminal side of the channel to maintain
the membranes permeability barrier.
• At some point , the channel opens laterally, and the hydrophobic helix is
inserted into the bilayer.(step 6).
•Step 6 shows the final deposition of the protein.
11.
12.
13. As each protein is synthesized in the rough ER, it becomes
inserted into the lipid bilayer in a predictable orientation
determined by its amino acid sequence.
14. Most membrane proteins function in the
following capacities: as receptors, as channels
or transporters, or as agents that transfer
electrons during the processes of
photosynthesis and respiration, and provides
strength.
15. Cell & Molecular Biology 5th edition Gerald
Karp
Molecular Cell Biology 6th edition Harvey
Lodish
The Cell A Molecular Approach 4th edition
Geoffrey M Cooper
Internet sources