Operon Concept

SET-1
1. Operon is a cluster of genes under control of a single promoter.
2. Jacob and Monod proposed the operon model.
3. Lac operon is an example of inducible operon.
4. Tryptophan operon is an example of repressible operon.
5. In lac operon, structural genes are lacZ, lacY, lacA.
6. LacZ encodes β-galactosidase.
7. LacY encodes permease.
8. LacA encodes transacetylase.
9. LacI is a regulator gene producing repressor protein.
10. Operator is the site where repressor binds.
11. Promoter is the site where RNA polymerase binds.
12. Inducer of lac operon is allolactose.
13. In absence of lactose, lac operon remains off.
14. In presence of lactose, repressor is inactivated.
15. cAMP-CRP complex enhances lac operon transcription.
16. Tryptophan operon has 5 structural genes.
17. In presence of tryptophan, trp operon is repressed.
18. Attenuation regulates trp operon transcription.
19. Arabinose operon is regulated both positively and negatively.
20. Operons are common in prokaryotes, rare in eukaryotes.

Transcription (Prokaryotes)

21. RNA polymerase holoenzyme in prokaryotes has α2ββ'σ subunits.

22. Core enzyme lacks σ factor.
23. σ factor helps in promoter recognition.
24. -10 region of promoter is Pribnow box (TATAAT).
25. -35 region sequence is TTGACA.
26. Transcription starts at +1 site.
27. Rho-independent termination involves hairpin loop.
28. Rho-dependent termination requires rho factor (ρ protein).
29. Rho factor is a helicase.
30. mRNA in prokaryotes is polycistronic.

Transcription (Eukaryotes)

31. RNA polymerase I synthesizes rRNA (28S, 18S, 5.8S).

32. RNA polymerase II synthesizes mRNA.
33. RNA polymerase III synthesizes tRNA and 5S rRNA.
34. Eukaryotic promoter has TATA box (Goldberg-Hogness box).
35. CAAT box occurs at -75 region.
36. Enhancers increase transcription efficiency.
 37. Silencers suppress transcription.
38. General transcription factors help RNA Pol II initiation.
39. TFIIH has helicase and kinase activity.
40. Transcription unit = promoter + coding region + terminator.

Regulatory Sequences & Factors

41. Enhancers act in cis-position.

42. Activators bind to enhancers.
43. Repressors bind to silencers/operators.
44. Co-activators bridge activators and transcription complex.
45. Co-repressors inhibit transcription via repressors.
46. Inducible genes are expressed in response to stimuli.
47. Housekeeping genes are constitutively expressed.
48. Eukaryotic transcription is monocistronic.
49. Mediator complex links activators and RNA Pol II.
50. Epigenetic modifications regulate gene expression.

Post-Transcriptional Modifications

51. 5’ capping protects mRNA from degradation.

52. Cap structure is 7-methylguanosine.
53. Polyadenylation adds poly(A) tail at 3’ end.
54. Poly(A) tail increases mRNA stability.
55. RNA splicing removes introns.
56. Exons are coding sequences.
57. Introns are non-coding sequences.
58. Spliceosome carries out RNA splicing.
59. Alternative splicing generates protein diversity.
60. RNA editing alters nucleotide sequence post-transcriptionally.

Protein Transport

61. Signal peptides direct proteins to ER.

62. Signal recognition particle (SRP) guides ribosomes to ER.
63. Nuclear localization signal (NLS) helps nuclear protein transport.
64. Proteins enter mitochondria via TOM and TIM complexes.
65. Secretory proteins follow ER → Golgi → Vesicles → Membrane route.

DNA-Protein Interaction

66. Helix-turn-helix motif is common in DNA-binding proteins.

67. Zinc finger motif binds DNA using zinc ion.
68. Leucine zipper motif forms dimeric transcription factors.
69. DNA-protein interactions control transcription regulation.
70. DNA-binding domains recognize specific base sequences.

Genetic Code

71. Genetic code is triplet in nature.

 72. Codons are read in 5’ → 3’ direction.
73. Start codon is AUG (codes for methionine).
74. Stop codons are UAA, UAG, UGA.
75. Genetic code is universal.
76. Genetic code is degenerate.
77. Wobble hypothesis explains tRNA pairing flexibility.
78. UAA is called ochre codon.
79. UAG is called amber codon.
80. UGA is called opal codon.

Translation

81. Translation occurs on ribosomes.

82. Prokaryotic ribosome is 70S (50S + 30S).
83. Eukaryotic ribosome is 80S (60S + 40S).
84. Initiation codon in prokaryotes is AUG (fMet).
85. Shine-Dalgarno sequence helps ribosome binding in prokaryotes.
86. Kozak sequence aids initiation in eukaryotes.
87. tRNA carries amino acids to ribosome.
88. Anticodon recognizes codon on mRNA.
89. Aminoacyl-tRNA synthetase charges tRNA with amino acid.
90. Peptidyl transferase forms peptide bonds.

Translation Control

91. miRNA regulates translation by binding mRNA.

92. siRNA causes mRNA degradation.
93. Phosphorylation of initiation factors regulates translation.
94. Stress conditions reduce global translation.
95. Iron response element regulates ferritin mRNA translation.

Post-Translational Modifications

96. Phosphorylation regulates protein activity.

97. Glycosylation modifies proteins for secretion.
98. Ubiquitination targets proteins for degradation.
99. Proteolytic cleavage activates zymogens.
100. Acetylation regulates chromatin binding proteins.
Operon Concept (continued)
SET-2
101. The repressor protein binds operator region to block transcription.
102. Allolactose acts as inducer in lac operon.
103. Catabolite repression keeps lac operon off in presence of glucose.
104. cAMP levels are inversely proportional to glucose concentration.
105. CAP (catabolite activator protein) enhances lac operon transcription.
106. CAP binds upstream of promoter in lac operon.
107. Arabinose operon uses AraC protein for regulation.
108. AraC acts as activator in presence of arabinose.
109. AraC acts as repressor in absence of arabinose.
110. Trp repressor binds operator only when bound to tryptophan.
111. Leader peptide regulates attenuation in trp operon.
112. Attenuation depends on ribosome stalling.
113. His operon is regulated by attenuation as well.
114. Multiple operons can be regulated by one regulator protein.
115. Regulon = set of operons controlled by single regulatory protein.
116. Lac operon is an example of negative inducible regulation.
117. Trp operon is negative repressible regulation.
118. Positive control requires activator proteins.
119. Negative control requires repressor proteins.
120. Polygenic mRNA encodes multiple proteins in prokaryotes.

Prokaryotic Transcription (advanced)

121. RNA polymerase in E. coli has no proofreading activity.

122. NusA stabilizes hairpin structure in termination.
123. σ70 is the housekeeping sigma factor.
124. Alternative sigma factors regulate stress genes.
125. σ32 regulates heat shock response.
126. σ54 regulates nitrogen metabolism genes.
127. Transcription bubble is ~17 bp long.
128. Rho factor is an ATP-dependent helicase.
129. Prokaryotic transcription and translation are coupled.
130. Polycistronic mRNA saves energy in bacteria.

Eukaryotic Transcription (advanced)

131. RNA Pol II needs TFIID for initiation.

132. TBP (TATA binding protein) is part of TFIID.
133. TFIIA stabilizes TBP binding.
134. TFIIB helps recruit RNA Pol II.
135. TFIIE recruits TFIIH.
136. TFIIH unwinds DNA and phosphorylates CTD of RNA Pol II.
 137. CTD = Carboxy terminal domain.
138. Phosphorylation of CTD is required for promoter clearance.
139. Enhancers can function even at large distances.
140. Insulators block enhancer action.
141. Histone acetylation increases transcription.
142. Histone deacetylation decreases transcription.
143. DNA methylation usually silences genes.
144. CpG islands are sites of DNA methylation.
145. Chromatin remodeling proteins regulate transcription.
146. Euchromatin is transcriptionally active.
147. Heterochromatin is transcriptionally inactive.
148. RNA Pol I transcription occurs in nucleolus.
149. RNA Pol III transcription occurs in nucleoplasm.
150. snRNA genes are transcribed by RNA Pol III.

Post-Transcriptional Modifications (detailed)

151. Capping occurs co-transcriptionally.

152. Poly(A) polymerase adds adenine residues.
153. CPSF recognizes AAUAAA signal.
154. GU-AG rule is common in intron splicing.
155. Branch point contains adenine.
156. U1 snRNP binds to 5’ splice site.
157. U2 snRNP binds branch site.
158. U4/U6 and U5 form spliceosome complex.
159. Alternative splicing can generate thousands of isoforms.
160. β-thalassemia is caused by defective splicing.
161. Self-splicing introns occur in rRNA.
162. Group I introns require guanosine as cofactor.
163. Group II introns use lariat mechanism.
164. RNA editing in trypanosomes uses guide RNAs.
165. ApoB mRNA editing creates shorter isoform in intestine.
166. mRNA transport involves nuclear pore complex.
167. Exon junction complex is added during splicing.
168. Nonsense-mediated decay degrades faulty mRNAs.
169. RNA interference is a post-transcriptional control.
170. piRNAs silence transposons.

Protein Transport & Sorting

171. Secretory proteins have N-terminal signal peptides.

172. SRP halts translation until ribosome binds ER.
173. ER signal is cleaved by signal peptidase.
174. Proteins move from ER → Golgi via COPII vesicles.
175. Golgi to ER transport uses COPI vesicles.
176. Clathrin vesicles transport proteins to lysosomes.
177. Mannose-6-phosphate directs proteins to lysosome.
178. KDEL sequence retains proteins in ER.
179. Mitochondrial matrix proteins unfold before import.
180. Nuclear proteins require NLS (nuclear localization signal).
181. NES (nuclear export signal) helps nuclear export.
 182. Peroxisomal proteins use SKL signal.
183. Protein disulfide isomerase helps folding in ER.
184. Chaperonins assist protein folding.
185. HSP70 family prevents misfolding.
186. HSP90 assists signaling protein folding.
187. Unfolded protein response (UPR) is activated by ER stress.
188. Proteasome degrades misfolded proteins.
189. Proteins are ubiquitinated before degradation.
190. N-glycosylation occurs in ER.

DNA-Protein Interaction (detailed)

191. HTH motif is common in prokaryotic repressors.

192. Zinc finger motif binds DNA bases via cysteine/histidine.
193. Basic helix-loop-helix (bHLH) motif aids dimerization.
194. Leucine zipper forms coiled-coil structure.
195. DNA-protein interactions can be studied by EMSA.
196. DNase footprinting identifies binding sites.
197. Chromatin immunoprecipitation (ChIP) maps protein-DNA binding.
198. DNA-binding proteins regulate transcription initiation.
199. Homeodomain proteins control developmental genes.
200. Transcription factors often have modular domains.
Genetic Code (expanded)
SET-3
201. The genetic code was deciphered by Nirenberg and Khorana.
202. Genetic code has 64 codons.
203. 61 codons code for amino acids.
204. 3 codons are stop codons.
205. Methionine is the universal initiator in eukaryotes.
206. fMet is the initiator in prokaryotes.
207. Genetic code is commaless.
208. Genetic code is non-overlapping.
209. Genetic code is colinear with polypeptide sequence.
210. Degeneracy provides mutation tolerance.
211. Single codon = one amino acid (unambiguous).
212. Wobble base is at 3rd position of codon.
213. Inosine at wobble position pairs with A, U, or C.
214. Some codons are assigned differently in mitochondria.
215. UGA codes for tryptophan in mitochondria.
216. Codon usage bias exists among organisms.
217. Synonymous codons code same amino acid.
218. Nonsense mutation creates premature stop codon.
219. Missense mutation changes amino acid.
220. Silent mutation does not change amino acid.

Translation Initiation

221. Translation requires ribosomes, tRNA, mRNA, initiation factors.

222. In prokaryotes, initiation requires IF1, IF2, IF3.
223. IF2 binds GTP and initiator tRNA.
224. Shine-Dalgarno sequence base pairs with 16S rRNA.
225. Start codon AUG codes for fMet in bacteria.
226. Initiation complex includes 30S, mRNA, fMet-tRNA.
227. 50S subunit joins to form 70S initiation complex.
228. In eukaryotes, initiation requires eIFs.
229. eIF2 binds initiator tRNA (Met).
230. eIF4E binds 5’ cap of mRNA.
231. Kozak sequence helps recognition of start codon.
232. 43S pre-initiation complex scans mRNA for AUG.
233. Large subunit (60S) joins after start codon recognition.
234. Initiation ends with hydrolysis of GTP.
235. Initiation is the rate-limiting step of translation.
236. Ribosome has A (aminoacyl), P (peptidyl), E (exit) sites.
237. Start codon sets the reading frame.
238. Prokaryotic translation begins even before transcription ends.
239. Eukaryotic translation is uncoupled from transcription.
 240. Polysomes are multiple ribosomes on same mRNA.

Translation Elongation

241. Elongation uses elongation factors.

242. In prokaryotes, EF-Tu delivers aminoacyl-tRNA to A site.
243. EF-Tu requires GTP hydrolysis.
244. EF-Ts regenerates EF-Tu-GTP.
245. EF-G mediates ribosome translocation.
246. Peptidyl transferase forms peptide bond.
247. Peptidyl transferase is a ribozyme (23S rRNA).
248. Growing polypeptide is transferred to tRNA at A site.
249. Ribosome moves 5’ → 3’ along mRNA.
250. Elongation cycle consumes 2 GTP per amino acid.
251. Accuracy depends on codon-anticodon pairing.
252. Kinetic proofreading enhances fidelity.
253. Error rate in translation is ~10⁻⁴.
254. Aminoacyl-tRNA synthetase ensures correct charging.
255. Ribosome protects ~30 nucleotides of mRNA.
256. Translocation shifts tRNA from A → P → E sites.
257. E site releases uncharged tRNA.
258. Translation elongates from N-terminus to C-terminus.
259. GTP hydrolysis provides energy for elongation.
260. Ribosome stalls at rare codons.

Translation Termination

261. Stop codons are recognized by release factors.

262. In prokaryotes, RF1 recognizes UAA, UAG.
263. RF2 recognizes UAA, UGA.
264. RF3 assists release factor recycling.
265. In eukaryotes, eRF1 recognizes all stop codons.
266. eRF3 is a GTPase aiding termination.
267. Hydrolysis releases polypeptide chain.
268. Ribosomal subunits dissociate after termination.
269. Ribosome recycling factor (RRF) helps disassembly.
270. Termination requires energy from GTP hydrolysis.

Translation Regulation

271. Global translation downregulated under starvation.

272. Phosphorylation of eIF2α inhibits initiation.
273. IRES (internal ribosome entry site) allows cap-independent initiation.
274. Viruses often use IRES for protein synthesis.
275. Ferritin mRNA is regulated by iron availability.
276. Low iron = IRP binds IRE → blocks translation.
277. High iron = IRP releases → translation proceeds.
278. Prokaryotic attenuation regulates translation-transcription coupling.
279. Riboswitches control gene expression via metabolite binding.
280. miRNA represses translation by base-pairing with 3’ UTR.
 281. siRNA induces mRNA cleavage.
282. RNA interference is a defense mechanism.
283. Translational control is rapid and reversible.
284. Stress granules store untranslated mRNAs.
285. mTOR pathway regulates protein synthesis in eukaryotes.
286. mTOR activation enhances ribosome biogenesis.
287. Phosphorylation of 4E-BP regulates eIF4E availability.
288. Global translation decreases during apoptosis.
289. Some viral proteins shut down host translation.
290. Prokaryotic ribosome-binding sites are essential for control.

Post-Translational Modifications

291. PTMs alter protein activity, stability, or localization.

292. Phosphorylation is catalyzed by kinases.
293. Dephosphorylation is by phosphatases.
294. Acetylation neutralizes lysine charges.
295. Histone acetylation opens chromatin.
296. Deacetylation condenses chromatin.
297. Ubiquitination tags proteins for degradation.
298. SUMOylation regulates nuclear proteins.
299. Glycosylation occurs on asparagine (N-linked) or serine/threonine (O-linked).
300. Myristoylation attaches fatty acid for membrane targeting.
 SET-4
Post-Translational Modifications (continued)

301. Palmitoylation attaches palmitic acid to cysteine.

302. Prenylation anchors proteins to membranes.
303. Hydroxylation of proline/lysine occurs in collagen.
304. Vitamin C is cofactor for prolyl hydroxylase.
305. Carboxylation of glutamate occurs in clotting factors.
306. γ-carboxyglutamate binds calcium.
307. Disulfide bonds stabilize protein structure.
308. Chaperones assist in folding after translation.
309. Proteolytic cleavage activates insulin.
310. Zymogens are inactive precursors of enzymes.
311. Glycosylphosphatidylinositol (GPI) anchors proteins to membranes.
312. N-acetylation of histones regulates chromatin.
313. Lipidation aids membrane targeting.
314. Nitrosylation modifies cysteine residues.
315. Methylation occurs on histones and transcription factors.
316. Citrullination modifies arginine residues.
317. O-GlcNAcylation regulates signaling proteins.
318. S-nitrosylation regulates redox proteins.
319. PTMs create protein diversity beyond genetic code.
320. PTMs are often reversible and dynamic.

Regulation of Gene Expression (Prokaryotes)

321. Negative control = repressor binding operator.

322. Positive control = activator enhancing transcription.
323. Catabolite repression = glucose inhibits other sugar utilization.
324. Stringent response reduces rRNA synthesis under starvation.
325. ppGpp mediates stringent response.
326. Attenuation links translation with transcription.
327. Feedback inhibition regulates operons.
328. Heat shock genes induced by σ32.
329. Sporulation genes induced by σF, σE.
330. Quorum sensing regulates group gene expression.
331. Autoinducers trigger quorum sensing.
332. Bioluminescence in Vibrio controlled by quorum sensing.
333. Riboswitches sense metabolites and alter mRNA structure.
334. Leader peptides regulate amino acid operons.
335. Translational coupling links adjacent cistrons.
336. Antitermination allows read-through transcription.
337. Phage λ uses antitermination proteins N and Q.
338. Phage λ lytic/lysogenic switch is classic regulation.
339. Cro protein favors lysis; CI favors lysogeny.
 340. Inducible operons respond to substrates.

Regulation of Gene Expression (Eukaryotes)

341. Cis-elements = promoters, enhancers, silencers.

342. Trans-factors = transcription factors.
343. General TFs are needed for basal transcription.
344. Specific TFs regulate tissue-specific genes.
345. Enhancers can function upstream or downstream.
346. Silencers reduce gene expression.
347. Insulators block enhancer-promoter interaction.
348. Chromatin state regulates transcription.
349. DNA methylation silences gene promoters.
350. CpG demethylation activates transcription.
351. Imprinting is parent-specific gene expression.
352. X-inactivation silences one X chromosome.
353. lncRNAs regulate chromatin state.
354. Xist RNA mediates X-inactivation.
355. Enhancer RNAs (eRNAs) modulate enhancer function.
356. Chromatin looping brings enhancers to promoters.
357. SWI/SNF remodels nucleosomes.
358. Histone acetylation increases accessibility.
359. Histone methylation can activate or repress.
360. HATs add acetyl groups; HDACs remove them.

Transcription Factors (Eukaryotes)

361. TFs have DNA-binding domain and activation domain.

362. Homeobox genes encode transcription factors for development.
363. p53 is a transcription factor regulating cell cycle.
364. NF-κB regulates immune response genes.
365. Steroid receptors are ligand-activated TFs.
366. Estrogen receptor binds estrogen response elements.
367. Glucocorticoid receptor binds GREs.
368. Heat shock factor binds HSEs.
369. bZIP proteins dimerize via leucine zipper.
370. bHLH proteins control differentiation.
371. STAT proteins mediate cytokine signaling.
372. CREB binds cAMP response elements.
373. Myc is a proto-oncogene transcription factor.
374. AP-1 is a dimer of Fos and Jun proteins.
375. Oct4 regulates stem cell pluripotency.
376. Sox2 works with Oct4 in pluripotency.
377. HIF-1 regulates hypoxia response.
378. TFs often require co-activators.
379. Mediator complex is central co-activator.
380. Co-repressors recruit HDACs.
DNA–Protein Interaction (advanced)

381. EMSA detects DNA-binding proteins.

382. DNase I footprinting shows binding sites.
383. ChIP maps binding in vivo.
384. HTH motif found in lac repressor.
385. Zinc fingers common in eukaryotic TFs.
386. Leucine zipper = hydrophobic leucines every 7 residues.
387. Homeodomain proteins control body plan genes.
388. Helix-loop-helix aids dimerization and DNA binding.
389. DNA-protein interactions stabilize transcription complexes.
390. Sequence-specific binding regulates expression precisely.

Translation & Protein Quality Control

391. Ribosome quality control degrades stalled mRNAs.

392. tmRNA rescues stalled ribosomes in bacteria.
393. No-go decay targets stalled ribosomes in eukaryotes.
394. Non-stop decay degrades mRNA lacking stop codons.
395. Nonsense-mediated decay eliminates premature stop codons.
396. Chaperones prevent aggregation during folding.
397. Proteasome degrades misfolded proteins.
398. UPR relieves ER stress by halting translation.
399. Heat shock proteins stabilize unfolded proteins.
400. Protein folding errors cause diseases like Alzheimer’s.
Translation Regulation (extra)
SET-5
401. Global translation is tightly linked to nutrient availability.
402. Amino acid starvation activates GCN2 kinase.
403. GCN2 phosphorylates eIF2α to reduce translation.
404. Viral IRES elements bypass cap recognition.
405. Poliovirus uses IRES for translation.
406. Hepatitis C virus translation uses IRES.
407. Stress granules store untranslated mRNA under stress.
408. P-bodies degrade mRNAs not needed.
409. Riboswitches alter secondary structure to regulate translation.
410. Translational pausing regulates co-translational folding.

Post-Translational Fate

411. Proteins fold during synthesis on ribosome.

412. Misfolded proteins are recognized by chaperones.
413. ERAD (ER-associated degradation) clears misfolded ER proteins.
414. Proteins targeted to proteasome are polyubiquitinated.
415. Lysosome degrades extracellular and membrane proteins.
416. Autophagy degrades bulk cytoplasmic proteins.
417. SUMOylation modifies nuclear transport proteins.
418. Lipidation anchors proteins in membranes.
419. Glycosylation affects protein stability and secretion.
420. PTMs regulate signaling cascades.

Gene Expression in Development

421. HOX genes control body patterning.

422. Mutations in HOX genes cause developmental defects.
423. Sonic hedgehog (Shh) gene regulates limb development.
424. Pax6 controls eye development.
425. MyoD regulates muscle differentiation.
426. Oct4, Sox2, Nanog maintain pluripotency.
427. Epigenetic regulation guides differentiation.
428. Enhancers drive tissue-specific expression.
429. Insulators prevent inappropriate activation.
430. Morphogens regulate gene expression gradients.

Epigenetic Regulation

431. DNA methylation is catalyzed by DNA methyltransferases.

432. Demethylation can be active or passive.
433. Histone methylation can activate (H3K4) or repress (H3K9).
 434. Histone acetyltransferases (HATs) activate genes.
435. Histone deacetylases (HDACs) repress genes.
436. Epigenetic changes are heritable.
437. Environmental factors alter epigenome.
438. Imprinting disorders include Prader-Willi and Angelman syndromes.
439. Epigenetic reprogramming occurs in germ cells.
440. Cancer often involves epigenetic dysregulation.

DNA–Protein Interaction (methods & importance)

441. SELEX identifies DNA-binding motifs.

442. Yeast one-hybrid screens DNA-protein interactions.
443. EMSA shift indicates DNA binding.
444. ChIP-seq maps genome-wide TF binding.
445. DNA-binding proteins regulate replication and repair too.
446. TBP bends DNA for transcription initiation.
447. HMG proteins modify DNA flexibility.
448. Architectural proteins organize chromatin domains.
449. Nucleosome positioning affects TF binding.
450. TF cooperativity increases binding specificity.

Genetic Code (repeated focus)

451. AUG is universal start codon.

452. Prokaryotic initiator tRNA carries formyl-methionine.
453. Mitochondrial code differs slightly from nuclear.
454. Genetic code is mostly universal.
455. Degeneracy protects against point mutations.
456. Third base wobble reduces tRNA requirement.
457. Frameshift mutations alter reading frame.
458. Codons are read without gaps.
459. Codons overlap only in rare viral genomes.
460. Genetic code established experimentally with synthetic RNA.

Translation Errors & Proofreading

461. Missense errors substitute wrong amino acid.

462. Nonsense errors create truncated proteins.
463. Suppressor tRNAs insert amino acids at stop codons.
464. Translational proofreading ensures fidelity.
465. Kinetic proofreading uses GTP hydrolysis.
466. Mistranslation rate ~1 in 10,000 codons.
467. Ribosome quality control pathways fix stalled translation.
468. Nonsense-mediated decay prevents faulty proteins.
469. Codon optimization improves heterologous expression.
470. Rare codons slow translation for folding.

Gene Expression in Eukaryotes – Advanced

471. Alternative promoters generate isoforms.

 472. Alternative splicing increases protein diversity.
473. RNA editing alters coding sequence post-transcriptionally.
474. Adenosine deamination converts A → I.
475. C-to-U editing changes cytidine to uridine.
476. miRNAs silence mRNAs post-transcriptionally.
477. siRNAs cause target mRNA cleavage.
478. piRNAs protect germline from transposons.
479. lncRNAs modulate chromatin state.
480. circRNAs regulate gene expression as sponges.

Operon & Regulation (revisited for reinforcement)

481. Lac operon inducible by lactose.

482. LacI repressor inhibits transcription.
483. Allolactose inactivates LacI repressor.
484. cAMP-CRP enhances lac transcription.
485. Trp operon repressed by tryptophan.
486. Attenuation fine-tunes trp operon regulation.
487. Arabinose operon activated by AraC-arabinose complex.
488. Riboswitches bind metabolites to regulate transcription/translation.
489. Negative regulation blocks transcription initiation.
490. Positive regulation enhances transcription initiation.

Post-Translational Modifications (repeated focus)

491. Ubiquitin-proteasome pathway degrades short-lived proteins.

492. Phosphorylation regulates enzyme activity.
493. Acetylation affects protein-protein interactions.
494. Glycosylation is common in secretory proteins.
495. Disulfide bonds form in ER lumen.
496. Lipidation targets proteins to membranes.
497. Hydroxylation stabilizes collagen structure.
498. Proteolysis activates hormones and enzymes.
499. SUMOylation regulates nuclear transport and DNA repair.
500. PTMs diversify protein function beyond genome instructions.