Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 5 de 5
Filter
Add more filters










Database
Language
Publication year range
1.
PLoS One ; 19(4): e0301642, 2024.
Article in English | MEDLINE | ID: mdl-38683832

ABSTRACT

Horizontal gene transfer (HGT) is a well-documented strategy used by bacteria to enhance their adaptability to challenging environmental conditions. Through HGT, a group of conserved genetic elements known as mobile genetic elements (MGEs) is disseminated within bacterial communities. MGEs offer numerous advantages to the host, increasing its fitness by acquiring new functions that help bacteria contend with adverse conditions, including exposure to heavy metal and antibiotics. This study explores MGEs within microbial communities along the Yucatan coast using a metatranscriptomics approach. Prior to this research, nothing was known about the coastal Yucatan's microbial environmental mobilome and HGT processes between these bacterial communities. This study reveals a positive correlation between MGEs and antibiotic resistance genes (ARGs) along the Yucatan coast, with higher MGEs abundance in more contaminated sites. The Proteobacteria and Firmicutes groups exhibited the highest number of MGEs. It's important to highlight that the most abundant classes of MGEs might not be the ones most strongly linked to ARGs, as observed for the recombination/repair class. This work presents the first geographical distribution of the environmental mobilome in Yucatan Peninsula mangroves.


Subject(s)
Gene Transfer, Horizontal , Interspersed Repetitive Sequences , Microbiota , Interspersed Repetitive Sequences/genetics , Microbiota/genetics , Mexico , Bacteria/genetics , Bacteria/classification , Proteobacteria/genetics
2.
Front Microbiol ; 13: 972267, 2022.
Article in English | MEDLINE | ID: mdl-36325016

ABSTRACT

Antibiotic resistance (AR) is one of the greatest human and clinical challenges associated with different pathogenic organisms. However, in recent years it has also become an environmental problem due to the widespread use of antibiotics in humans and livestock activities. The ability to resist antibiotics comes from antibiotic resistance genes (ARGs) and our understanding of their presence in coastal environments is still limited. Therefore, the objective of the present study was to explore the presence and possible differences in the microbial resistome of four sites from the Yucatan coast through the evaluation of the composition and abundance of ARGs using a high-throughput analysis of metatranscriptomic sequences. In total, 3,498 ARGs were uncovered, which participate in the resistance to tetracycline, macrolide, rifamycin, fluoroquinolone, phenicol, aminoglycoside, cephalosporin, and other antibiotics. The molecular mechanisms of these ARGs were mainly efflux pump, antibiotic target alteration and antibiotic target replacement. In the same way, ARGs were detected in the samples but showing dissimilar enrichment levels. With respect to the sampling sites, the ARGs were present in all the samples collected, either from preserved or contaminated areas. Importantly, sediments of the preserved area of Dzilam presented the second highest level of ARGs detected, probably as a consequence of the antibiotics dragged to the coast by submarine groundwater discharge. In general, the resistance to a single antibiotic was greater than multiresistance, both at the level of gene and organisms; and multiresistance in organisms is acquired mainly by recruiting different monoresistance genes. To our knowledge, this is the first study that describes and compares the resistome of different samples of the Yucatan coast. This study contributes to generating information about the current state of antibiotic resistance on the Yucatan coasts for a better understanding of ARGs dissemination and could facilitate the management of ARGs pollution in the environment.

3.
Int J Mol Sci ; 22(23)2021 Dec 03.
Article in English | MEDLINE | ID: mdl-34884901

ABSTRACT

The process of phase separation allows for the establishment and formation of subcompartmentalized structures, thus enabling cells to perform simultaneous processes with precise organization and low energy requirements. Chemical modifications of proteins, RNA, and lipids alter the molecular environment facilitating enzymatic reactions at higher concentrations in particular regions of the cell. In this review, we discuss the nucleolus as an example of the establishment, dynamics, and maintenance of a membraneless organelle with a high level of organization.


Subject(s)
Cell Nucleolus/metabolism , Intrinsically Disordered Proteins/isolation & purification , Intrinsically Disordered Proteins/metabolism , Gene Expression Regulation , Humans , Liquid-Liquid Extraction , Nuclear Proteins/isolation & purification , Nuclear Proteins/metabolism
4.
Cells ; 9(5)2020 05 06.
Article in English | MEDLINE | ID: mdl-32384686

ABSTRACT

Fibrillarin is a highly conserved nucleolar methyltransferase responsible for ribosomal RNA methylation across evolution from Archaea to humans. It has been reported that fibrillarin is involved in the methylation of histone H2A in nucleoli and other processes, including viral progression, cellular stress, nuclear shape, and cell cycle progression. We show that fibrillarin has an additional activity as a ribonuclease. The activity is affected by phosphoinositides and phosphatidic acid and insensitive to ribonuclease inhibitors. Furthermore, the presence of phosphatidic acid releases the fibrillarin-U3 snoRNA complex. We show that the ribonuclease activity localizes to the GAR (glycine/arginine-rich) domain conserved in a small group of RNA interacting proteins. The introduction of the GAR domain occurred in evolution in the transition from archaea to eukaryotic cells. The interaction of this domain with phospholipids may allow a phase separation of this protein in nucleoli.


Subject(s)
Chromosomal Proteins, Non-Histone/chemistry , Chromosomal Proteins, Non-Histone/metabolism , Phospholipids/metabolism , Ribonucleases/chemistry , Ribonucleases/metabolism , Chromosomal Proteins, Non-Histone/genetics , HeLa Cells , Humans , Mutation/genetics , Protein Domains , RNA, Small Nucleolar/metabolism , Recombinant Proteins/metabolism , Ribonucleases/genetics , Ribonucleoproteins/metabolism , Structure-Activity Relationship
5.
Protein Expr Purif ; 136: 45-51, 2017 Aug.
Article in English | MEDLINE | ID: mdl-28624494

ABSTRACT

The gene of the four disulfide-bridged defensin J1-1 from Capsicum was cloned into the expression vector pQE30 containing a 6His-tag as fusion protein. This construct was transfected into Origami strain of Escherichia coli and expressed after induction with isopropyl thiogalactoside (IPTG). The level of expression was 4 mg/L of culture medium, and the His-tagged recombinant defensin (HisXarJ1-1) was expressed exclusively into inclusion bodies. After solubilization, HisXarJ1-1 was purified by affinity and hydrophobic interaction chromatography. The reverse-phase HPLC profile of the HisXarJ1-1 product obtained from the affinity chromatography step showed single main peptide fraction of molecular masses of 7050.6 Da and after treatment with DTT a single fraction of 7, 042.6 Da corresponding to the reduced peptide was observed. An in vitro folding step of the HisXarJ1-1 generated a distinct profile of oxidized forms of the peptide this oxidized peptide was capable of binding phosphatidic acid in vitro. Possible dimer and oligomer of HisXarJ1-1 were visible in gel electrophoresis and immunodetected with anti-His antibodies. Pure recombinant defensin HisXarJ1-1 exhibited antibacterial activity against Pseudomonas aeruginosa.


Subject(s)
Anti-Bacterial Agents , Capsicum/genetics , Defensins , Plant Proteins , Pseudomonas aeruginosa/growth & development , Anti-Bacterial Agents/biosynthesis , Anti-Bacterial Agents/isolation & purification , Anti-Bacterial Agents/pharmacology , Capsicum/metabolism , Defensins/biosynthesis , Defensins/genetics , Defensins/isolation & purification , Defensins/pharmacology , Escherichia coli/genetics , Escherichia coli/metabolism , Inclusion Bodies/chemistry , Inclusion Bodies/genetics , Inclusion Bodies/metabolism , Plant Proteins/biosynthesis , Plant Proteins/genetics , Plant Proteins/isolation & purification , Plant Proteins/pharmacology , Recombinant Proteins/biosynthesis , Recombinant Proteins/genetics , Recombinant Proteins/isolation & purification , Recombinant Proteins/pharmacology
SELECTION OF CITATIONS
SEARCH DETAIL
...