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foundation of practice > cell translation > Flashcards

cell translation Flashcards

1
Q

the major steps in info processing in bio are —– of genetic code and its —- into proteins

A
  • transcription
  • translation
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2
Q

the products of transcription aka —- are the starting material for —–

A
  • mrna
  • translation
    ( gene ( dna —> rna ( mrna , trna rrna) —> translation —> protein
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3
Q

—– refers to the info in mrna is trslatated into amino acids ( proteins )

A

translation

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4
Q

key components of translation:
1—– template , encodes info to make proteins
2—— carrier , each amino acid brought to mrna
3—– structural anf fucntional roles of ribosomes
4- —– proteins
5- —– factors

A
  • mrna
  • trna
    -rrnaaaaa
  • ribosomal proteins
  • translation/releasing factors
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5
Q

each word aka codon of the dna is consist of —-

A

3 nucleotide/bases = 1 amino acids
( we have 64 possiblikes bc we onlyy have 4 nucltodie and we have 20 amino acids )

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6
Q

—- refers to the first codon in protein
— refers to the stop codon

A
  • aug ( met )
  • UAA
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7
Q

— refers to the stating point of dna trasncprition while — is for the translation

A
  • ATG
  • AUG
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8
Q

—- refers to a set of codons that run continuously bounded by an imitation codon and termination codon

A

open reading frame ORF

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9
Q

——- is determined by which base is chosen as the start of the codon

A

reading frame

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10
Q

in protein synthesis usually only — ORF contains useful info

A

one

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11
Q

characteristics of the genetic code has to be:

A

1- specific: a specific codon always codes for the same aa
2- universal: applies to all species , conserved from early stages of evolution
3- reboundant: a given amino acid can be coded for by several different codons
5- non overlapping : the code is read from a fixed starting point , as continuous sequence of bases , taken 3 at a time

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12
Q

true or false:
- changes in the code can cause disease
- sometimes the codon can become amplified between generations as huntigtons disease the father carries 4 copies but passes 8 copies
- each copy of the codon = extra copy of aa in the protein which can cause a misfiled protein accumulation HTT protein /gene

A

all true

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13
Q

change in the codon can cause sickle cell anaemia which is the missense mutation in — gene which is a single subsitiun from —- in the codon of the amino acid — , it converts glutamic acid GAG to —- codon and its autosomal recessive

A
  • b globin gene
  • A to T
  • amino acid 6
  • valine code GTG
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14
Q

—- the dictionary that translates dna sequence into amino acids

A

genetic code

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15
Q

true or false:
amino acid binds to the acceptor arm , aminoacyl-trna sythetase couples amino acid to correct trna sequence
while anticodon arm base pairs w mrna sequence

A

true

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16
Q

—- contains amino acid and can recognise and bind to specific codons in the mrna transcript

A

trna

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17
Q

we have 50 trna matching 61 codons for 20 amino acids so trna can match to —- codon which is called —-

A
  • more than one codon
  • flexible pairing aka wobble which are the last 3’ base in codon on mean which binds to the first 5’ bases in anticodon in trna
18
Q

wobble base is the last — base in the codon on mrna and it binds with the first — on the anticodon of the trna
the wobble allows —– in use of trna and a single trna species carrying AA can recongzie —- condos

A
  • 3’
  • 5’
  • efficiency/ flexibility
  • 2
19
Q

—- are factories in which protein sytheiss occurs they are complexes of proteins and rna

A

ribosomes

20
Q

—- extensive secondary structuring similar to trna , ribosomal proteins interact w components of translation system

A
  • rrna
21
Q

—- brings mrna and trna together to translate nuceltodie sequence of mrna into amino acid of a protein.
it has 3 main sites which are:

A

ribosomes
- A site ( aminoacyl ) : acceptor site for the next trna
- P site ( peptide ) contains the amino acid chain
- E site ( exit ) harbours deacylate trna so its uncharged , on way out of ribosomes

22
Q

the initiator trna enters through — while all others enter through the a site

A

p site

23
Q

process of translation :
1- invitation which consists of 2 parts
a. assembly of components which require for chain formation which includes :
b. recognition of the start codon by the —-

A
  • 2 ribosomal subunit , mrna to be translated , trna specify by the first codon in the mrna , gap which provide energy , initiation factors that help ribosomes recognise the sequence for the start of the translation
  • trna met
24
Q

—- process involves the addition of amino acids to the c- terminus aka the carboxyl end of the growing peptide chain , ribosomes will move alone mrna being translated in —– direction

A
  • elnogation
  • 5-3
25
Q

process of translation:
2.elongation:
- next required aminoacytle-trna is delivered to a —- site w/ the help of elongation factors
- —- bonds formed between adjacent amino acids facilitated by the enzyme ——-
- after the bond is formed the ribosomes are —- the nucleotide in the 3’ direction aka to the right to the next codon . so the growing chain is moved to —- site , uncharged trna moves to —- site and the A site is — to accept next trna

A
  • a site
    -peptide bond
    -peptidyltransferase
  • translocated
  • p site
  • e site
  • free
26
Q

—– occurs when one of the three termination codons arrives in the a site , stops codon recognised by —- factors , release factors bind to —- which causes :
- newly sytehsised protein to be released
- diassembly of the trna-ribsome-mran complex

A
  • termination
  • releasing
  • a site
27
Q

true or false: Cells are not static – need to change and adapt to
environmental stimulus very rapidly

A

true

28
Q

1-the regulating protein levels mechanism:
2.how can we regulate protein activity:

A

1a- increased transcprtion/ translation enhances levels
1b- degradation removes protein when function complete or damaged
- * Protein levels
* Protein location and concentration
* Ligand Binding
* Cofactor requirements. Eg: Ca2+ or GTP
* Post-translational modifications

29
Q

—- is a normal process that ensures a protein fit for a purpose but its also a mechanism that can be used to — a pathway , — activity or – a process

A
  • protein turnover
  • shut off
  • reduce
  • stop
30
Q

proteins with a key —– often rapidly turned over or degraded to keep the, under tight regulation

A

regulatory functions

31
Q

proteins get degraded when :
1——– turnover which refers to the housekeeping proteins get damaged and need replacing or the misfiled proteins need to be recycled
2- —– is when the levels of proteins tightly regulated to control fucntion as cyclins are synthesised to promote entry into cell cycle and rare degraded when want to turn them off also it occurs in the course of being activated some proteins get cleaved and need to be replaced as : digestive enzymes that are secreted as zymogens

A

1- normal protein turnover
2- dynamic process - turning on/off highly regulated

32
Q

—- degrades proteins that are imported into the cells and is not specific
—- degrades systolic proteins marked for destruction

A

1- lysosomal degradation
2- proteasomal degradation

33
Q

—- protects the cytosolic proteins from activities if they leak out and they degrade any biological material as protein nucleic acid carbs lipid

A

lysosomes pr

34
Q

—- when proteins are labeled or tagged for degradation

A

‘polyubiquitination’ aka in proteasomal degradation and it targets protein that is rcohnzied

35
Q

—–a multiprotein, barrel shaped
complex containing protease enzymes
*Found in the nucleus or cytoplasm
*Same basic composition all sub-types and
same function – protein degradation

A

protesome

36
Q

Common post-translational modifications (PTMs):

A

– Ligand binding
– Phosphorylation
– Cleavage to produce active protein/enzyme
– Ubiquitination
– Fatty acid modification/ lipidation
– Glycosylation

37
Q

—- changes the shape of protein , active conformation , release of inhibitory subunits and change of cell location
as: steroid hormone binding their ligands, gets conformational change m now dimerise and enters the nucleas

A

ligand binding

38
Q

Zymogens – pro-enzymes
Cleavage of pro-enzymes activates refers to:

A

proteolytic cleavage

39
Q

reversible phosphorylation of proteins:
- phsosphate group added to —— and their ratios are:
—– mat be least abundant but has the most effect

A
  • serine:theronine:tyrosine S:T: Y
  • ratios : 100:10:1
  • trysoine
40
Q

in reversible phosphorylation of proteins they are very — regulated and —– added to phosphate and —- remove it

A
  • tightly
  • kinasase
  • phosphatase
41
Q

fucntions of phosphorylation :

A
  • alters protein function
  • marks for degradation
  • alters localisation
  • promotes interactions
    ( check slide 37 + 38 plsssss)

foundation of practice (59 decks)

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