Cargando…
Self-assembly of proteins and their nucleic acids
We have developed an artificial protein scaffold, herewith called a protein vector, which allows linking of an in-vitro synthesised protein to the nucleic acid which encodes it through the process of self-assembly. This protein vector enables the direct physical linkage between a functional protein...
Autores principales: | , , , |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2003
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC151556/ https://www.ncbi.nlm.nih.gov/pubmed/12646068 http://dx.doi.org/10.1186/1477-3155-1-1 |
_version_ | 1782120675860807680 |
---|---|
author | Fletcher, Graham Mason, Sean Terrett, Jon Soloviev, Mikhail |
author_facet | Fletcher, Graham Mason, Sean Terrett, Jon Soloviev, Mikhail |
author_sort | Fletcher, Graham |
collection | PubMed |
description | We have developed an artificial protein scaffold, herewith called a protein vector, which allows linking of an in-vitro synthesised protein to the nucleic acid which encodes it through the process of self-assembly. This protein vector enables the direct physical linkage between a functional protein and its genetic code. The principle is demonstrated using a streptavidin-based protein vector (SAPV) as both a nucleic acid binding pocket and a protein display system. We have shown that functional proteins or protein domains can be produced in vitro and physically linked to their DNA in a single enzymatic reaction. Such self-assembled protein-DNA complexes can be used for protein cloning, the cloning of protein affinity reagents or for the production of proteins which self-assemble on a variety of solid supports. Self-assembly can be utilised for making libraries of protein-DNA complexes or for labelling the protein part of such a complex to a high specific activity by labelling the nucleic acid associated with the protein. In summary, self-assembly offers an opportunity to quickly generate cheap protein affinity reagents, which can also be efficiently labelled, for use in traditional affinity assays or for protein arrays instead of conventional antibodies. |
format | Text |
id | pubmed-151556 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2003 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-1515562003-03-18 Self-assembly of proteins and their nucleic acids Fletcher, Graham Mason, Sean Terrett, Jon Soloviev, Mikhail J Nanobiotechnology Research We have developed an artificial protein scaffold, herewith called a protein vector, which allows linking of an in-vitro synthesised protein to the nucleic acid which encodes it through the process of self-assembly. This protein vector enables the direct physical linkage between a functional protein and its genetic code. The principle is demonstrated using a streptavidin-based protein vector (SAPV) as both a nucleic acid binding pocket and a protein display system. We have shown that functional proteins or protein domains can be produced in vitro and physically linked to their DNA in a single enzymatic reaction. Such self-assembled protein-DNA complexes can be used for protein cloning, the cloning of protein affinity reagents or for the production of proteins which self-assemble on a variety of solid supports. Self-assembly can be utilised for making libraries of protein-DNA complexes or for labelling the protein part of such a complex to a high specific activity by labelling the nucleic acid associated with the protein. In summary, self-assembly offers an opportunity to quickly generate cheap protein affinity reagents, which can also be efficiently labelled, for use in traditional affinity assays or for protein arrays instead of conventional antibodies. BioMed Central 2003-01-28 /pmc/articles/PMC151556/ /pubmed/12646068 http://dx.doi.org/10.1186/1477-3155-1-1 Text en Copyright © 2003 Fletcher et al; licensee BioMed Central Ltd. This is an Open Access article: verbatim copying and redistribution of this article are permitted in all media for any purpose, provided this notice is preserved along with the article's original URL. |
spellingShingle | Research Fletcher, Graham Mason, Sean Terrett, Jon Soloviev, Mikhail Self-assembly of proteins and their nucleic acids |
title | Self-assembly of proteins and their nucleic acids |
title_full | Self-assembly of proteins and their nucleic acids |
title_fullStr | Self-assembly of proteins and their nucleic acids |
title_full_unstemmed | Self-assembly of proteins and their nucleic acids |
title_short | Self-assembly of proteins and their nucleic acids |
title_sort | self-assembly of proteins and their nucleic acids |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC151556/ https://www.ncbi.nlm.nih.gov/pubmed/12646068 http://dx.doi.org/10.1186/1477-3155-1-1 |
work_keys_str_mv | AT fletchergraham selfassemblyofproteinsandtheirnucleicacids AT masonsean selfassemblyofproteinsandtheirnucleicacids AT terrettjon selfassemblyofproteinsandtheirnucleicacids AT solovievmikhail selfassemblyofproteinsandtheirnucleicacids |