High Incidence of Disorder-Promoting Amino Acids in the Amino Terminus of Mature Proteins in Bacillus subtilis

Guangqiang Wang; Yining Dong; Haiqin Chen; Heping Zhang; Yuanda Song; Hao Zhang; Wei Chen

doi:10.3844/ajbbsp.2011.172.178

Article Details

High Incidence of Disorder-Promoting Amino Acids in the Amino Terminus of Mature Proteins in Bacillus subtilis

Authors:

Guangqiang Wang | Yining Dong | Haiqin Chen | Heping Zhang | Yuanda Song | Hao Zhang | Wei Chen

Publisher:

Science Publications

Journal:

American Journal of Biochemistry and Biotechnology Vol.7 Issue 4, pp.172-178

Document Type:

Article

Publication Date:

2/2012

Document Language:

English

Document ID (Org No.):

2001397085

pISSN:

1558-6332

DOI:

10.3844/ajbbsp.2011.172.178

Keywords:

Abstract:

 Problem statement: Exported polypeptides are usually synthesized as preproteins which are composed with mature domains and the signal peptides. The foreign proteins are usually inefficiently secreted by the aid of signal peptides. Although we know that the mature protein played an important role in the protein export process, we do not know what properties of the mature domains are critical for protein export? This study explores the influence of the property of the mature domains on protein export in Bacillus subtilis. Approach: We analyzed the amino acid composition of 241 predicted exported proteins and 457 cytoplasmic proteins of Bacillus subtilis that have been previously reviewed using the program DAMBE, Codeprotein and Codeprotein Win. Results: Disorder-promoting amino acids in the first 14 residues of the mature domains were overrepresented in comparison to the residues in the NH2-terminal region of cytoplasmic proteins or the cytoplasmic proteins. Further, the NH2 terminus of the mature domain had more negatively charged residues and fewer positively charged residues than the NH2 terminus of the signal peptide. Conclusion/Recommendations: The presence of disordered domains in the NH2-terminal regions of mature domains may provide the binding site and maintain the exported proteins in a secretion-competent conformation and the contrary charged residues distribution in the two ends of hydrophobic core may help form the hairpin-like structure of the signal peptide. These findings may have important implications for the understanding of the contribution of mature domains to membrane targeting and to translocation.

Article Details

High Incidence of Disorder-Promoting Amino Acids in the Amino Terminus of Mature Proteins in Bacillus subtilis

Authors:

Guangqiang Wang | Yining Dong | Haiqin Chen | Heping Zhang | Yuanda Song | Hao Zhang | Wei Chen

Publisher:

Science Publications

Journal:

American Journal of Biochemistry and Biotechnology Vol.7 Issue 4, pp.172-178

Document Type:

Article

Publication Date:

2/2012

Document Language:

English

Document ID (Org No.):

2001397085

pISSN:

1558-6332

DOI:

10.3844/ajbbsp.2011.172.178

Protein export

disorder-promoting amino acid

mature domain

signal peptide

Bacillus subtilis

hydrophobic core

charged residues

hairpin-like structure

disordered domains

Issues

Article Details

Authors: Guangqiang Wang | Yining Dong | Haiqin Chen | Heping Zhang | Yuanda Song | Hao Zhang | Wei Chen

Publisher: Science Publications

Journal: American Journal of Biochemistry and Biotechnology Vol.7 Issue 4, pp.172-178

Document Type: Article

Publication Date: 2/2012

Document Language: English

Document ID (Org No.): 2001397085

pISSN: 1558-6332

DOI: 10.3844/ajbbsp.2011.172.178

Issues

Authors:

Guangqiang Wang | Yining Dong | Haiqin Chen | Heping Zhang | Yuanda Song | Hao Zhang | Wei Chen

Publisher:

Science Publications

Journal:

American Journal of Biochemistry and Biotechnology Vol.7 Issue 4, pp.172-178

Document Type:

Article

Publication Date:

2/2012

Document Language:

English

Document ID (Org No.):

2001397085

pISSN:

1558-6332

DOI:

10.3844/ajbbsp.2011.172.178