拉索生物合成中的领导的去除,基于前最后一个异黄素残留物
Yuwei Duan1, Weijing Niu1, Linlin Pang1
1Helmholtz International Laboratory for Anti-Infectives, State Key Laboratory of Microbial Technology, Shandong University, Qingdao, China.
Frontiers in microbiology
|July 27, 2023
概括
这项研究确定了Bradymonas sediminis中的一种新型拉索前体,具有独特的前期异氨酸残留物. 这一发现挑战了先前对拉索处理和基质特异性的理解.
科学领域:
- 微生物学 微生物学
- 生物化学 生物化学
- 分子生物学分子生物学
背景情况:
- 拉索是通过核糖体合成的,具有独特的拉里亚特拓,由翻译后修改形成.
- 带头的去除和核心的宏分离是拉索成熟的关键步骤.
- 在领导的前后位置保存的三氨酸残留物通常对酶处理至关重要.
研究的目的:
- 为了研究布拉迪莫纳斯 sediminis FA350.的拉索的生物合成.
- 描述在领导加工中的前最后一个残留物的作用.
- 为了识别新的拉索前体及其相关酶.
主要方法:
- 在Bradymonas sediminis.中识别了拉索生物合成基因集群 (bsf).
- 酵素测试以研究酸化和领导的去除.
- 在基分析的拉索前体序列.
主要成果:
- 在Bradymonas sediminis中发现了一种新的拉索前体BsfA.
- 酶BsfK在Ser3残留物中化BsfA. 在Ser3残留物中化BsfA.
- BsfB1和BsfB2酶参与了领导的去除,由于前最后一个异黄素残留物,表现出改变了基质选择性.
- 这是第一个实验验证在拉索前体中的前最后一个异黄素的验证.
结论:
- 在BsfA中最后一个前期的异黄素残留物显著影响酸化和领导的去除,表明BsfB1和BsfB2的新基质选择性.
- 这一发现扩大了已知的拉索前体和加工机制的多样性.
- 这些发现表明,前后Ile/Val残留物虽然很少见,但在不同细菌序列的化拉索中存在.
更多相关视频
08:48Specificity Analysis of Protein Lysine Methyltransferases Using SPOT Peptide Arrays
Published on: November 29, 2014
14.0K
12:02An Efficient Method for the Synthesis of Peptoids with Mixed Lysine-type/Arginine-type Monomers and Evaluation of Their Anti-leishmanial Activity
Published on: November 2, 2016
12.1K
相关概念视频
Leaky Scanning
5.2K
During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA. Marilyn Kozak discovered that the sequence RCCAUGG (where R...
5.2K
Directing Proteins to the Rough Endoplasmic Reticulum
7.3K
The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
7.3K
ER Retrieval Pathway
3.9K
In the secretory pathway, vesicles transport proteins from one cellular compartment to another in forward transport to deliver the protein to its correct location. Occasionally, misfolded proteins and incorrect proteins escape their original compartments, and a retrieval pathway is used to return the escaped proteins to their original compartment.
The ER uses many checkpoints to prevent the entry of incorrectly folded or a resident protein as cargo onto a transport vesicle. These mechanisms...
The ER uses many checkpoints to prevent the entry of incorrectly folded or a resident protein as cargo onto a transport vesicle. These mechanisms...
3.9K
Cotranslational Protein Translocation
7.4K
Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
7.4K
Translocation of Proteins into the Mitochondria
3.2K
Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
3.2K
