Abstract: To produce a bacterial microcompartment shell, or a designed shell based on naturally occurring bacterial microcompartment shells in a new host organism, a synthetic operon is constructed that contains the desired shell protein genes and translation efficiency is controlled by host specific ribosomal binding sites. Proteins or other molecules can be encapsulated in the microcompartment shells by various methods described herein. The constructs can also be used to express self-assembling sheets comprised of shell proteins.

Abstract: To produce a bacterial microcompartment shell, or a designed shell based on naturally occurring bacterial microcompartment shells in a new host organism, a synthetic operon is constructed that contains the desired shell protein genes and translation efficiency is controlled by host specific ribosomal binding sites. Proteins or other molecules can be encapsulated in the microcompartment shells by various methods described herein. The constructs can also be used to express self-assembling sheets comprised of shell proteins.

Abstract: A conserved region of sequence in bacterial microcompartment (BMC) enzymes and proteins was identified. Peptide sequences derived from this conserved region of native BMC proteins and enzymes appear to target the hexameric facets of BMC shell proteins. These peptides were predicted to share general properties of a predicted alpha helical conformation, flanked by poorly conserved segment(s) of primary structure); for each type of encapsulated protein, and for each functionally distinct BMC. These peptides can be used as targeting signals for integrating biomolecules and molecules into bacterial microcompartments or for attaching molecules or biomolecules to native or non-native bacterial microcompartment shell proteins.

Abstract: To produce a bacterial microcompartment shell, or a designed shell based on naturally occurring bacterial microcompartment shells in a new host organism, a synthetic operon is constructed that contains the desired shell protein genes and translation efficiency is controlled by host specific ribosomal binding sites. Proteins or other molecules can be encapsulated in the microcompartment shells by various methods described herein. The constructs can also be used to express self-assembling sheets comprised of shell proteins.

Abstract: A conserved region of sequence in bacterial microcompartment (BMC) enzymes and proteins was identified. Peptide sequences derived from this conserved region of native BMC proteins and enzymes appear to target the hexameric facets of BMC shell proteins. These peptides were predicted to share general properties of a predicted alpha helical conformation, flanked by poorly conserved segment(s) of primary structure); for each type of encapsulated protein, and for each functionally distinct BMC. These peptides can be used as targeting signals for integrating biomolecules and molecules into bacterial microcompartments or for attaching molecules or biomolecules to native or non-native bacterial microcompartment shell proteins.