Bacterial species exhibit diversity in their mechanisms and capacity for protein disulfide bond formation.
نویسندگان
چکیده
Protein disulfide bond formation contributes to the folding and activity of many exported proteins in bacteria. However, information about disulfide bond formation is limited to only a few bacterial species. We used a multifaceted bioinformatic approach to assess the capacity for disulfide bond formation across this biologically diverse group of organisms. We combined data from a cysteine counting method, in which a significant bias for even numbers of cysteine in proteins is taken as an indicator of disulfide bond formation, with data on the presence of homologs of known disulfide bond formation enzymes. These combined data enabled us to make predictions about disulfide bond formation in the cell envelope across bacterial species. Our bioinformatic and experimental results suggest that many bacteria may not generally oxidatively fold proteins, and implicate the bacterial homolog of the enzyme vitamin K epoxide reductase, a protein required for blood clotting in humans, as part of a disulfide bond formation pathway present in several major bacterial phyla.
منابع مشابه
Diversity of the Epsilonproteobacteria Dsb (disulfide bond) systems
The bacterial proteins of the Dsb family-important components of the post-translational protein modification system-catalyze the formation of disulfide bridges, a process that is crucial for protein structure stabilization and activity. Dsb systems play an essential role in the assembly of many virulence factors. Recent rapid advances in global analysis of bacteria have thrown light on the enor...
متن کاملEnhanced Solubility of Anti-HER2 scFv Using Bacterial Pelb Leader Sequence
Single chain Fragment variable (scFv) is an antibody fragment consisting variable regions of heavy and light chains. scFvs enhance their penetrability into tissues while maintaining specific affinity and having low immunogenicity. Insoluble inclusion bodies are formed when scFvs are expressed in reducing bacterial cytoplasm. One strategy for obtaining functionally active scFv is to translocate ...
متن کاملRecombinant Production of a Novel Fusion Protein: Listeriolysin O Fragment Fused to S1 Subunit Of Pertussis Toxin
Background: Some resources have suggested that genetically inactivated pertussis toxoid (PTs) bear a more protective effect than chemically inactivated products. This study aimed to produce new version of PT, by cloning an inactive pertussis toxin S1 subunit (PTS1) in a fusion form with N-terminal half of the listeriolysin O (LLO) pore-forming toxin. Methods: Deposited pdb structure file of the...
متن کاملBridge over Troubled Waters Sensing Stress by Disulfide Bond Formation
are members of the thioredoxin superfamily and exert their action by a disulfide exchange reaction utilizing a Cys-X1-X2-Cys active site. Other members of the thioredoxin superfamily are responsible for the introduction and isomerization of disulfide bonds that are often presFredrik Åslund† and Jon Beckwith* Department of Microbiology and Molecular Genetics Harvard Medical School 200 Longwood A...
متن کاملThe Genomics of Disulfide Bonding and Protein Stabilization in Thermophiles
Thermophilic organisms flourish in varied high-temperature environmental niches that are deadly to other organisms. Recently, genomic evidence has implicated a critical role for disulfide bonds in the structural stabilization of intracellular proteins from certain of these organisms, contrary to the conventional view that structural disulfide bonds are exclusively extracellular. Here both compu...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Proceedings of the National Academy of Sciences of the United States of America
دوره 105 33 شماره
صفحات -
تاریخ انتشار 2008