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- Keyword
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- Acetobixan (1)
- Cell membranes (1)
- Cellulose biosynthesis inhibitor (1)
- HIV-1 (1)
- Histone-Lysine N-Methyltransferase (1)
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- Human immunodeficiency virus (HIV) (1)
- Humans (1)
- Jurkat Cells (1)
- Lysine (1)
- Methylation (1)
- Microbial Bioprospecting (1)
- Post-translational modification (PTM) (1)
- Protein methylation (1)
- Tat Gene Products, Human Immunodeficiency Virus (1)
- Transcription regulation (1)
- Transcriptional Activation (1)
- Viral transcription (1)
Articles 1 - 2 of 2
Full-Text Articles in Life Sciences
The Hiv-1 Tat Protein Is Monomethylated At Lysine 71 By The Lysine Methyltransferase Kmt7, Ibraheem Ali, Holly Ramage, Daniela Boehm, Lynnette M. A. Dirk, Naoki Sakane, Kazuki Hanada, Sara Pagans, Katrin Kaehlcke, Katherine Aull, Leor Weinberger, Raymond Trievel, Martina Schnoelzer, Masafumi Kamada, Robert L. Houtz, Melanie Ott
The Hiv-1 Tat Protein Is Monomethylated At Lysine 71 By The Lysine Methyltransferase Kmt7, Ibraheem Ali, Holly Ramage, Daniela Boehm, Lynnette M. A. Dirk, Naoki Sakane, Kazuki Hanada, Sara Pagans, Katrin Kaehlcke, Katherine Aull, Leor Weinberger, Raymond Trievel, Martina Schnoelzer, Masafumi Kamada, Robert L. Houtz, Melanie Ott
Horticulture Faculty Publications
The HIV-1 transactivator protein Tat is a critical regulator of HIV transcription primarily enabling efficient elongation of viral transcripts. Its interactions with RNA and various host factors are regulated by ordered, transient post-translational modifications. Here, we report a novel Tat modification, monomethylation at lysine 71 (K71). We found that Lys-71 monomethylation (K71me) is catalyzed by KMT7, a methyltransferase that also targets lysine 51 (K51) in Tat. Using mass spectrometry, in vitro enzymology, and modification-specific antibodies, we found that KMT7 monomethylates both Lys-71 and Lys-51 in Tat. K71me is important for full Tat transactivation, as KMT7 knockdown impaired the transcriptional activity …
Acetobixan, An Inhibitor Of Cellulose Synthesis Identified By Microbial Bioprospecting, Ye Xia, Lei Lei, Chad Brabham, Jozsef Stork, James R. Strickland, Adam Ladak, Ying Gu, Ian Wallace, Seth Debolt
Acetobixan, An Inhibitor Of Cellulose Synthesis Identified By Microbial Bioprospecting, Ye Xia, Lei Lei, Chad Brabham, Jozsef Stork, James R. Strickland, Adam Ladak, Ying Gu, Ian Wallace, Seth Debolt
Horticulture Faculty Publications
In plants, cellulose biosynthesis is an essential process for anisotropic growth and therefore is an ideal target for inhibition. Based on the documented utility of small-molecule inhibitors to dissect complex cellular processes we identified a cellulose biosynthesis inhibitor (CBI), named acetobixan, by bio-prospecting among compounds secreted by endophytic microorganisms. Acetobixan was identified using a drug-gene interaction screen to sift through hundreds of endophytic microbial secretions for one that caused synergistic reduction in root expansion of the leaky AtcesA6prc1-1 mutant. We then mined this microbial secretion for compounds that were differentially abundant compared with Bacilli that failed to mimic CBI action …