Unlabelled: Free -4-hydroxy-L-proline (T4LHyp), a non-proteinogenic amino acid, is mainly released from the degradation of collagen, hydroxyproline-rich glycoproteins, and some peptide antibiotics in nature. Although it has been known that some terrestrial bacteria utilize T4LHyp as carbon and nitrogen source via a T4LHyp gene cluster, which and how marine microorganisms catabolize T4LHyp still remains unclear. Here, five T4LHyp-utilizing marine bacterial strains, sp. 5021, sp. 4072, sp. 6022, sp. 5112 and sp. 30521, were isolated from hydrothermal vent sediment samples collected from the southwest Indian Ocean. While sp. 5021 can utilize T4LHyp as both a nitrogen and carbon source, the other four strains can utilize T4LHyp as only a nitrogen source. Then, the T4LHyp catabolic mechanisms of sp. 5021 and sp. 4072, as a representative of the four strains, were further investigated by genomic, transcriptional, and biochemical analyses. sp. 5021 adopts an intact T4LHyp gene cluster containing four enzymes to catabolize T4LHyp into NH and α-ketoglutarate to provide nitrogen and carbon sources for its growth. Compared to sp. 5021, sp. 4072 lacks an α-KGSA dehydrogenase gene in the T4LHyp gene cluster and can only catabolize T4LHyp into NH and α-ketoglutarate semialdehyde to provide a nitrogen source for its growth. Bioinformatic investigation showed that the 5021-like and 4072-like T4LHyp gene clusters are predominantly found in bacteria from , which are widely distributed in multiple marine habitats. Thus, bacteria are likely the dominant group to drive the recycling and mineralization of T4LHyp in the ocean.
Supplementary Information: The online version contains supplementary material available at 10.1007/s42995-024-00272-8.
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http://dx.doi.org/10.1007/s42995-024-00272-8 | DOI Listing |
Mar Life Sci Technol
February 2025
State Key Laboratory of Microbial Technology, Shandong University, Qingdao, 266237 China.
Unlabelled: Free -4-hydroxy-L-proline (T4LHyp), a non-proteinogenic amino acid, is mainly released from the degradation of collagen, hydroxyproline-rich glycoproteins, and some peptide antibiotics in nature. Although it has been known that some terrestrial bacteria utilize T4LHyp as carbon and nitrogen source via a T4LHyp gene cluster, which and how marine microorganisms catabolize T4LHyp still remains unclear. Here, five T4LHyp-utilizing marine bacterial strains, sp.
View Article and Find Full Text PDFBiosci Biotechnol Biochem
January 2018
a Department of Bioscience, Graduate School of Agriculture , Ehime University, Matsuyama , Japan.
The hypO gene from Sinorhizobium meliloti, located within the trans-4-hydroxy-L-proline metabolic gene cluster, was first successfully expressed in the host Pseudomonas putida. Purified HypO protein functioned as a FAD-containing cis-4-hydroxy-D-proline dehydrogenase with a homomeric structure. In contrast to other known enzymes, significant activity for D-proline was found, confirming a previously proposed potential involvement in D-proline metabolism.
View Article and Find Full Text PDFJ Bacteriol
August 2017
Department of Bioscience, Graduate School of Agriculture, Ehime University, Matsuyama, Ehime, Japan.
Hydroxyprolines, such as -4-hydroxy-l-proline (T4LHyp), -3-hydroxy-l-proline (T3LHyp), and -3-hydroxy-l-proline (C3LHyp), are present in some proteins including collagen, plant cell wall, and several peptide antibiotics. In bacteria, genes involved in the degradation of hydroxyproline are often clustered on the genome (l-Hyp gene cluster). We recently reported that an aconitase X (AcnX)-like gene from an l-Hyp gene cluster functions as a monomeric C3LHyp dehydratase (AcnX).
View Article and Find Full Text PDFFEBS Open Bio
March 2014
Faculty of Agriculture, Ehime University, 3-5-7 Tarumi, Matsuyama, Ehime 790-8566, Japan.
trans-4-Hydroxy-l-proline (T4LHyp) and trans-3-hydroxy-l-proline (T3LHyp) occur mainly in collagen. A few bacteria can convert T4LHyp to α-ketoglutarate, and we previously revealed a hypothetical pathway consisting of four enzymes at the molecular level (J Biol Chem (2007) 282, 6685-6695; J Biol Chem (2012) 287, 32674-32688). Here, we first found that Azospirillum brasilense has the ability to grow not only on T4LHyp but also T3LHyp as a sole carbon source.
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