Hygromycin B

Catalog No.S2908 Batch:S290806

Technical Data

Formula	C₂₀H₃₇N₃O₁₃
Molecular Weight	527.52	CAS No.	31282-04-9
Solubility (25°C)*	In vitro	Water	100 mg/mL (189.56 mM)
		DMSO	Insoluble
		Ethanol	Insoluble
* <1 mg/ml means slightly soluble or insoluble. * Please note that Selleck tests the solubility of all compounds in-house, and the actual solubility may differ slightly from published values. This is normal and is due to slight batch-to-batch variations. * Room temperature shipping (Stability testing shows this product can be shipped without any cooling measures.)

Preparing Stock Solutions

Biological Activity

Description	Hygromycin B (Hygrovetine), a selective antibiotic that is effective on most bacteria, fungi and higher eukaryotes, inhibits protein synthesis by interfering with translocation and causing mistranslation at the 70S ribosome.
In vitro	Hygromycin B has a single binding site within the 30S, it locates in the major groove of the helix very close to the helical axis, and makes contact with nucleotides from both RNA strands in the region 1490-1500 and 1400–1410. Ring I of HygB is involved in nonsequence-specific interactions with the backbone phosphate oxygen atoms of G1494 in addition to base-specific interactions with G1494 and U1495. Rings II and III make weak base-specific hydrogen bonds to both C1404 and U1498, but their main role apparently is to position ring IV for interaction with bases in the 1496–1498 region. Ring IV of HygB comes within 4A of the second base of the P site bound mRNA codon. ^[1] Hygromycin B (0.38 mM) completely halts yeast cell growth in rich media. Hygromycin B strongly block Polypeptide synthesis in cell-free extracts from rabbit reticulocytes, wheat germ and yeast. Hygromycin B inhibits peptide chain elongation by yeast polysomes by preventing elongation factor EF-2-dependent translocation. ^[2] Hygromycin B inhibits (80%) the elogation-factor-(EF)G-plus-GTP-dependent reaction of either AcPhe-tRNA or natural peptideyl-tRNA with puromycin in Escherichia coli cell-free systems. Hygromycin B blocks the nascnet peptide chains of either purified endogenous E. coli polysomes or poly(uridylic acid)-programmed ribosomes during polypeptide synthesis. Hygromycin B inhibits the non-enzymic translocation and the release of AcPhe-tRNA from the ribosomal acceptor site promoted by depletion of NH4 ions. ^[3] Hygromycin B is used for resistance selection in mouse L cells transfected with Escherichia coli genes coding for resistance to the aminocyclitol antibiotics hygromycin B. ^[4] Hygromycin B is used as a selectable marker for T-DNA transfer and integration in the ectomycorrhizal fungus Suillus bovinus. ^[5]

Description

Hygromycin B (Hygrovetine), a selective antibiotic that is effective on most bacteria, fungi and higher eukaryotes, inhibits protein synthesis by interfering with translocation and causing mistranslation at the 70S ribosome.

In vitro

Hygromycin B has a single binding site within the 30S, it locates in the major groove of the helix very close to the helical axis, and makes contact with nucleotides from both RNA strands in the region 1490-1500 and 1400–1410. Ring I of HygB is involved in nonsequence-specific interactions with the backbone phosphate oxygen atoms of G1494 in addition to base-specific interactions with G1494 and U1495. Rings II and III make weak base-specific hydrogen bonds to both C1404 and U1498, but their main role apparently is to position ring IV for interaction with bases in the 1496–1498 region. Ring IV of HygB comes within 4A of the second base of the P site bound mRNA codon. ^[1]

Hygromycin B (0.38 mM) completely halts yeast cell growth in rich media. Hygromycin B strongly block Polypeptide synthesis in cell-free extracts from rabbit reticulocytes, wheat germ and yeast. Hygromycin B inhibits peptide chain elongation by yeast polysomes by preventing elongation factor EF-2-dependent translocation. ^[2]

Hygromycin B inhibits (80%) the elogation-factor-(EF)G-plus-GTP-dependent reaction of either AcPhe-tRNA or natural peptideyl-tRNA with puromycin in Escherichia coli cell-free systems. Hygromycin B blocks the nascnet peptide chains of either purified endogenous E. coli polysomes or poly(uridylic acid)-programmed ribosomes during polypeptide synthesis. Hygromycin B inhibits the non-enzymic translocation and the release of AcPhe-tRNA from the ribosomal acceptor site promoted by depletion of NH4 ions. ^[3]

Hygromycin B is used for resistance selection in mouse L cells transfected with Escherichia coli genes coding for resistance to the aminocyclitol antibiotics hygromycin B. ^[4]

Hygromycin B is used as a selectable marker for T-DNA transfer and integration in the ectomycorrhizal fungus Suillus bovinus. ^[5]

Protocol (from reference)

References

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Selleck's Hygromycin B has been cited by 11 publications

UBR5 mediates colorectal cancer chemoresistance by attenuating ferroptosis via Lys 11 ubiquitin-dependent stabilization of Smad3-SLC7A11 signaling [ Redox Biol, 2024, 76:103349]	PubMed: 39260061
The xenobiotic transporter ABCC4/MRP4 promotes epithelial mesenchymal transition in pancreatic cancer [ Front Pharmacol, 2024, 15:1432851]	PubMed: 39114357
APOBEC3B coordinates R-loop to promote replication stress and sensitize cancer cells to ATR/Chk1 inhibitors [ Cell Death Dis, 2023, 14(6):348]	PubMed: 37270643
APOBEC3B coordinates R-loop to promote replication stress and sensitize cancer cells to ATR/Chk1 inhibitors [ Cell Death Dis, 2023, 14(6):348]	PubMed: 37270643
Detection of Alternative End-Joining in HNSC Cell Lines Using DNA Double-Strand Break Reporter Assays [ Bio Protoc, 2022, 12(17)e4506]	PubMed: 36213110
CGAS is a micronucleophagy receptor for the clearance of micronuclei [ Autophagy, 2021, 1-17]	PubMed: 33752561
The RNA helicase DDX5 promotes viral infection via regulating N6-methyladenosine levels on the DHX58 and NFκB transcripts to dampen antiviral innate immunity [ PLoS Pathog, 2021, 17(4):e1009530]	PubMed: 33909701
[ Cell Res, 2020, ]	PubMed: 32839552
SETDB1-Mediated Cell Fate Transition between 2C-Like and Pluripotent States. [ Cell Rep, 2020, 30(1):25-36]	PubMed: 31914391
[ Sci Rep, 2020, ]	PubMed: 32848164

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