ArticleFunctional & integrative genomics2009
Bacterial intein-like domains of predatory bacteria: a new domain type characterized in Bdellovibrio bacteriovorus.
Article in Functional & integrative genomics, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
7 citing papers in PubMed, 18 citations in OpenAlex.
- A unique self-truncation of bacterial GH5 endoglucanases leads to enhanced activity and thermostability.BMC biology · 2022Article
- Bacterial genome instability.Microbiology and molecular biology reviews : MMBR · 2014Review
- The role of reticulate evolution in creating innovation and complexity.International journal of evolutionary biology · 2012Article
- A three-way comparative genomic analysis of Mannheimia haemolytica isolates.BMC genomics · 2010Article
- Article
- Conservation of intron and intein insertion sites: implications for life histories of parasitic genetic elements.BMC evolutionary biology · 2009Article
- Group I introns and inteins: disparate origins but convergent parasitic strategies.Journal of bacteriology · 2009Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We report a new family of bacterial intein-like domains (BILs) identified in ten proteins of four diverse predatory bacteria. BILs belong to the HINT (Hedgehog/Intein) superfamily of domains that post-translationally self-process their protein molecules by protein splicing and self-cleavage. The new, C-type, BILs appear with other domains, including putative predator-specific domain 1 (PPS-1), a new domain typically appearing immediately upstream of C-type BILs. The Bd2400 protein of the obligate predator Bdellovibrio bacteriovorus includes a C-type BIL and a PPS-1 domains at its C-terminal part, and a signal peptide and two polycystic kidney disease domains at its N-terminal part. We demonstrate the in vivo transcription, translation, secretion, and processing of the B. bacteriovorus protein, and the in vitro autocatalytic N-terminal cleavage activity of its C-type BIL. Interestingly, whereas the Bd2400 gene is constitutively expressed, its protein product is differentially processed throughout the dimorphic life cycle of the B. bacteriovorus predator. The modular structure of the protein, its localization, and complex processing suggest that it may be involved in the interaction between the predator and its prey.
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