<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>14</volume><submitter>Yuan S</submitter><pubmed_abstract>&lt;h4>Background&lt;/h4>Eukaryotic ubiquitin and SUMO are frequently used as tags to enhance the fusion protein expression in microbial host. They increase the solubility and stability, and protect the peptides from proteolytic degradation due to their stable and highly conserved structures. Few of prokaryotic ubiquitin-like proteins was used as fusion tags except ThiS, which enhances the fusion expression, however, reduces the solubility and stability of the expressed peptides in E. coli. Hence, we investigated if MoaD, a conserved small sulfur carrier in prokaryotes with the similar structure of ubiquitin, could also be used as fusion tag in heterologous expression in E. coli.&lt;h4>Results&lt;/h4>Fusion of MoaD to either end of EGFP enhanced the expression yield of EGFP with a similar efficacy of </pubmed_abstract><journal>BMC biotechnology</journal><pagination>5</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3906898</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Ubiquitin-like prokaryotic MoaD as a fusion tag for expression of heterologous proteins in Escherichia coli.</pubmed_title><pmcid>PMC3906898</pmcid><pubmed_authors>Yuan S</pubmed_authors><pubmed_authors>Wang N</pubmed_authors><pubmed_authors>Yan Z</pubmed_authors><pubmed_authors>Wang X</pubmed_authors><pubmed_authors>Xu J</pubmed_authors></additional><is_claimable>false</is_claimable><name>Ubiquitin-like prokaryotic MoaD as a fusion tag for expression of heterologous proteins in Escherichia coli.</name><description>&lt;h4>Background&lt;/h4>Eukaryotic ubiquitin and SUMO are frequently used as tags to enhance the fusion protein expression in microbial host. They increase the solubility and stability, and protect the peptides from proteolytic degradation due to their stable and highly conserved structures. Few of prokaryotic ubiquitin-like proteins was used as fusion tags except ThiS, which enhances the fusion expression, however, reduces the solubility and stability of the expressed peptides in E. coli. Hence, we investigated if MoaD, a conserved small sulfur carrier in prokaryotes with the similar structure of ubiquitin, could also be used as fusion tag in heterologous expression in E. coli.&lt;h4>Results&lt;/h4>Fusion of MoaD to either end of EGFP enhanced the expression yield of EGFP with a similar efficacy of </description><dates><release>2014-01-01T00:00:00Z</release><publication>2014 Jan</publication><modification>2025-04-05T11:49:20.799Z</modification><creation>2019-03-27T01:20:54Z</creation></dates><accession>S-EPMC3906898</accession><cross_references><pubmed>24444081</pubmed><doi>10.1186/1472-6750-14-5</doi></cross_references></HashMap>