A guanidine-degrading enzyme controls genomic stability of ethylene-producing cyanobacteria
نویسندگان
چکیده
Abstract Recent studies have revealed the prevalence and biological significance of guanidine metabolism in nature. However, metabolic pathways used by microbes to degrade or mitigate its toxicity not been widely studied. Here, via comparative proteomics subsequent experimental validation, we demonstrate that Sll1077, previously annotated as an agmatinase enzyme model cyanobacterium Synechocystis sp. PCC 6803, is more likely a guanidinase it can break down rather than agmatine into urea ammonium. The Synechococcus elongatus 7942 strain engineered express bacterial ethylene-forming (EFE) exhibits unstable ethylene production due genomic instability induced accumulation EFE-byproduct guanidine. Co-expression EFE Sll1077 significantly enhances stability enables resulting achieve sustained high-level production. These findings expand our knowledge natural degradation their biotechnological application support bioproduction.
منابع مشابه
Mesophilic cyanobacteria producing thermophilic restriction endonucleases.
When searching for the site-specific endonucleases in several strains of Phormidium we made the following observations. Among the 16 strains that originated from 15 species of Phormidium, 12 produced one or more restriction enzymes, of which two produced the highly thermophilic restriction endonucleases PtaI and PpaAII with their optimum activity at 65-80 degrees C, which is far above the letha...
متن کاملRubber-degrading enzyme from a bacterial culture.
Rubber-degrading activity was found in the extracellular culture medium of Xanthomonas sp. strain 35Y which was grown on natural rubber latex. Natural rubber in the latex state was degraded by the crude enzyme, and two fractions were separately observed by gel permeation chromatography of the reaction products. One fraction was of higher molecular weight (HMW) with a very wide MW distribution f...
متن کاملIsolation of a Penicillin Acylase Producing E.coli and Kinetic Characterization of the Whole Cell Enzyme Activity
Penicillin acylase (EC 3.5.1.11) has been a target of study for a long time because of its pivotal role in the deacylation of the penicillin into the 6- aminopenicillanic acid (6-APA) and the side-chain organic acids. This property of penicillin acylase has been exploited commercially for large scale production of 6-APA, which is the key intermediate in the manufacture of semi-synthetic penicil...
متن کاملDistribution of Hydrogenases in Cyanobacteria: A Phylum-Wide Genomic Survey
Microbial Molecular hydrogen (H2) cycling plays an important role in several ecological niches. Hydrogenases (H2ases), enzymes involved in H2 metabolism, are of great interest for investigating microbial communities, and producing BioH2. To obtain an overall picture of the genetic ability of Cyanobacteria to produce H2ases, we conducted a phylum wide analysis of the distribution of the genes en...
متن کاملAnatoxin-a producing Tychonema (Cyanobacteria) in European waterbodies.
In order to identify the cyanobacterial species responsible of anatoxin-a (ATX) production in Lake Garda (Northern Italy), an intensive isolation and culturing of filamentous cyanobacteria were established since 2014 from environmental samples. In this work, we report a detailed account of the strategy adopted, which led to the discovery of a new unexpected producer of ATX, Tychonema bourrellyi...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Nature Communications
سال: 2021
ISSN: ['2041-1723']
DOI: https://doi.org/10.1038/s41467-021-25369-x