Related Experiment Video
Updated: May 8, 2026

07:02
An Assay for Quantifying Protein-RNA Binding in Bacteria
Published on: June 12, 2019
PPR-SMRs: ancient proteins with enigmatic functions.
Sheng Liu1, Joanna Melonek1, Laura M Boykin2
1Australian Research Council Centre of Excellence in Plant Energy Biology; The University of Western Australia; Crawley, WA Australia.
RNA Biology
|September 6, 2013
Summary
Pentatricopeptide repeat-small MutS-related (PPR-SMR) proteins are crucial for chloroplast biogenesis and signaling in plants. Phylogenetic analysis reveals their ancient origins within the Viridiplantae clade.
Area of Science:
- Plant Biology
- Molecular Evolution
- Cellular Biology
Background:
- Pentatricopeptide repeat (PPR) proteins are a large family in plants.
- A small subset of PPR proteins possess a C-terminal small MutS-related (SMR) domain.
- These PPR-SMR proteins are significant in chloroplast biogenesis and retrograde signaling.
Purpose of the Study:
- To review current knowledge on PPR-SMR proteins.
- To analyze their occurrence and evolutionary history in Viridiplantae.
- To discuss their potential functions, including endonucleolytic activity.
Main Methods:
- Review of proteomic and mutant studies in Arabidopsis and maize.
- Phylogenetic analysis of PPR-SMR proteins across various organisms.
- Comparative analysis of SMR domain conservation.
Main Results:
- PPR-SMR proteins are found in species with chloroplasts.
- Phylogenetic analysis indicates early evolution of PPR-SMR proteins in the Viridiplantae clade.
- Conservation of SMR domains suggests potential shared functions, possibly endonucleolytic activity.
Conclusions:
- PPR-SMR proteins have a long evolutionary history within photosynthetic eukaryotes.
- Their conserved structure and potential functions highlight their importance in chloroplast biology.
- Further research is needed to fully elucidate the roles of these proteins.
Related Concept Videos
Ribozymes
The term ribozyme is used for RNA that can act as an enzyme. Ribozymes are mainly found in selected viruses, bacteria, plant organelles, and lower eukaryotes. Ribozymes were first discovered in 1982 when Tom Cech’s laboratory observed Group I introns acting as enzymes. This was shortly followed by the discovery of another ribozyme, Ribonulcease P, by Sid Altman’s laboratory. Both Cech and Altman received the Nobel Prize in chemistry in 1989 for their work on ribozymes.
Ribozymes can be...
Ribozymes can be...
Subviral Agents
Subviral agents are infectious entities that resemble viruses but lack one or more viral components, such as a capsid or essential replication machinery. These agents include viroids, prions, and satellites, each possessing distinct structural and functional characteristics that influence their mode of infection and replication.Viroids are the simplest subviral agents, consisting of circular, single-stranded RNA molecules without a protein coat. They exclusively infect plants, relying entirely...
Rous Sarcoma Virus (RSV) and Cancer
Rous Sarcoma virus or RSV was discovered by F. Peyton Rous in the year 1911 as a filterable transmissible agent that could cause tumors in chickens. He won a Nobel Prize for this discovery in 1966. His experiments clearly demonstrated that some cancers could be caused by infectious agents and led to the discovery of many more cancer-causing viruses in animals as well as humans.
RSV is a retrovirus that contains two copies of a plus-strand RNA genome. Its genome consists of four main open...
RSV is a retrovirus that contains two copies of a plus-strand RNA genome. Its genome consists of four main open...
Protein Families
Protein families are groups of homologous proteins; that is, they have similarities in amino acid sequences and three-dimensional structures. Protein families usually occur because of gene duplication, where an additional copy of a gene is inserted into the genome of an organism. Mutations that change the amino acids but still allow the protein to be properly synthesized, will lead to new protein family members. If these new proteins contain similar amino acids in key locations, protein...
Leaky Scanning
During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA. Marilyn Kozak discovered that the sequence RCCAUGG (where R stands for...
Directing Proteins to the Rough Endoplasmic Reticulum
The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...

