Impact of C‐terminal amino acid composition on protein expression in bacteria
Abstract The C‐terminal sequence of a protein is involved in processes such as efficiency of translation termination and protein degradation. However, the general relationship between features of this C‐terminal sequence and levels of protein expression remains unknown. Here, we identified C‐termina...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
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Springer Nature
2020-05-01
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| Series: | Molecular Systems Biology |
| Subjects: | |
| Online Access: | https://doi.org/10.15252/msb.20199208 |
| _version_ | 1797281838677360640 |
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| author | Marc Weber Raul Burgos Eva Yus Jae‐Seong Yang Maria Lluch‐Senar Luis Serrano |
| author_facet | Marc Weber Raul Burgos Eva Yus Jae‐Seong Yang Maria Lluch‐Senar Luis Serrano |
| author_sort | Marc Weber |
| collection | DOAJ |
| description | Abstract The C‐terminal sequence of a protein is involved in processes such as efficiency of translation termination and protein degradation. However, the general relationship between features of this C‐terminal sequence and levels of protein expression remains unknown. Here, we identified C‐terminal amino acid biases that are ubiquitous across the bacterial taxonomy (1,582 genomes). We showed that the frequency is higher for positively charged amino acids (lysine, arginine), while hydrophobic amino acids and threonine are lower. We then studied the impact of C‐terminal composition on protein levels in a library of Mycoplasma pneumoniae mutants, covering all possible combinations of the two last codons. We found that charged and polar residues, in particular lysine, led to higher expression, while hydrophobic and aromatic residues led to lower expression, with a difference in protein levels up to fourfold. We further showed that modulation of protein degradation rate could be one of the main mechanisms driving these differences. Our results demonstrate that the identity of the last amino acids has a strong influence on protein expression levels. |
| first_indexed | 2024-03-07T17:03:13Z |
| format | Article |
| id | doaj.art-bc9fa6fff7c64bb28736e9486cf34e50 |
| institution | Directory Open Access Journal |
| issn | 1744-4292 |
| language | English |
| last_indexed | 2024-03-07T17:03:13Z |
| publishDate | 2020-05-01 |
| publisher | Springer Nature |
| record_format | Article |
| series | Molecular Systems Biology |
| spelling | doaj.art-bc9fa6fff7c64bb28736e9486cf34e502024-03-03T03:13:02ZengSpringer NatureMolecular Systems Biology1744-42922020-05-01165n/an/a10.15252/msb.20199208Impact of C‐terminal amino acid composition on protein expression in bacteriaMarc Weber0Raul Burgos1Eva Yus2Jae‐Seong Yang3Maria Lluch‐Senar4Luis Serrano5Centre for Genomic Regulation (CRG) The Barcelona Institute of Science and Technology Barcelona SpainCentre for Genomic Regulation (CRG) The Barcelona Institute of Science and Technology Barcelona SpainCentre for Genomic Regulation (CRG) The Barcelona Institute of Science and Technology Barcelona SpainCentre for Genomic Regulation (CRG) The Barcelona Institute of Science and Technology Barcelona SpainCentre for Genomic Regulation (CRG) The Barcelona Institute of Science and Technology Barcelona SpainCentre for Genomic Regulation (CRG) The Barcelona Institute of Science and Technology Barcelona SpainAbstract The C‐terminal sequence of a protein is involved in processes such as efficiency of translation termination and protein degradation. However, the general relationship between features of this C‐terminal sequence and levels of protein expression remains unknown. Here, we identified C‐terminal amino acid biases that are ubiquitous across the bacterial taxonomy (1,582 genomes). We showed that the frequency is higher for positively charged amino acids (lysine, arginine), while hydrophobic amino acids and threonine are lower. We then studied the impact of C‐terminal composition on protein levels in a library of Mycoplasma pneumoniae mutants, covering all possible combinations of the two last codons. We found that charged and polar residues, in particular lysine, led to higher expression, while hydrophobic and aromatic residues led to lower expression, with a difference in protein levels up to fourfold. We further showed that modulation of protein degradation rate could be one of the main mechanisms driving these differences. Our results demonstrate that the identity of the last amino acids has a strong influence on protein expression levels.https://doi.org/10.15252/msb.20199208bacteriabiasC‐terminaldegradationexpression |
| spellingShingle | Marc Weber Raul Burgos Eva Yus Jae‐Seong Yang Maria Lluch‐Senar Luis Serrano Impact of C‐terminal amino acid composition on protein expression in bacteria Molecular Systems Biology bacteria bias C‐terminal degradation expression |
| title | Impact of C‐terminal amino acid composition on protein expression in bacteria |
| title_full | Impact of C‐terminal amino acid composition on protein expression in bacteria |
| title_fullStr | Impact of C‐terminal amino acid composition on protein expression in bacteria |
| title_full_unstemmed | Impact of C‐terminal amino acid composition on protein expression in bacteria |
| title_short | Impact of C‐terminal amino acid composition on protein expression in bacteria |
| title_sort | impact of c terminal amino acid composition on protein expression in bacteria |
| topic | bacteria bias C‐terminal degradation expression |
| url | https://doi.org/10.15252/msb.20199208 |
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