Illustration of RimP protein assembling a ribosome within a bacterial cell.

Decoding Ribosomes: How a Key Protein Helps Build Cellular Factories

Soraya Malik in Science & Nature August 2025 • 4 min read.

"New research illuminates the crucial role of RimP in ribosome assembly, offering potential targets for fighting tuberculosis and other bacterial infections."

Ribosomes are the cell's protein factories, essential for life. Building these complex structures is a demanding task, requiring a host of helper molecules. One such helper, Ribosomal maturation factor P (RimP), is vital for ribosome assembly in bacteria. Understanding how RimP works is crucial, especially as it could provide new ways to combat bacterial infections.

A new study focuses on RimP, seeking to understand its structure and function in Mycobacterium smegmatis, a close relative of Mycobacterium tuberculosis, the bacterium that causes TB. Because TB is a major global health threat, understanding bacterial mechanisms is vital for creating new treatments.

This article breaks down the research, explaining how scientists have revealed RimP's structure and how it interacts with other components to facilitate ribosome assembly. This knowledge opens doors for developing drugs that specifically target RimP, potentially disrupting ribosome production and halting bacterial growth.

RimP's Structure: A Bridge Between Ribosome Components

Illustration of RimP protein assembling a ribosome within a bacterial cell.

The research team successfully determined the crystal structure of RimP from Mycobacterium smegmatis (MSMEG_2624). This revealed that RimP has two distinct domains connected by a flexible linker region. While the individual domains resemble a previously known structure, the way they are arranged and interact with each other was a novel finding.

Importantly, the researchers discovered that RimP interacts with a small ribosomal protein called S12 (RpsL). This interaction is critical for RimP's role in ribosome assembly. Further analysis pinpointed that the linker region between RimP's two domains is essential for this interaction with RpsL.

Here's a breakdown of the key findings:

RimP has two domains connected by a linker.
The linker region is crucial for binding to ribosomal protein S12 (RpsL).
Neither domain alone can strongly interact with RpsL; the entire RimP structure is needed.
Specific residues within the linker are essential for RpsL binding.

To confirm the importance of the linker region, scientists created mutant versions of RimP with alterations in this area. These mutants showed a significantly reduced ability to bind to RpsL, demonstrating the linker's critical role in coordinating the interaction. Further in-vivo analysis showed that this linker region is essential for the normal function of the ribosome.

A New Target for Fighting Bacterial Infections

This study provides a significant step forward in understanding how ribosomes are assembled in bacteria. By revealing the structure of RimP and its interaction with RpsL, the research highlights a potential target for new antibacterial drugs.

Because RimP is highly conserved in bacteria and absent in mammals, it represents an ideal target. Drugs that disrupt RimP's function could selectively inhibit bacterial ribosome production without harming human cells. This approach is particularly promising for combating drug-resistant bacteria like Mycobacterium tuberculosis.

The crystal structure of MSMEG_2624 now provides a template for designing drugs that specifically bind to and disrupt RimP's function. Further research in this area could lead to the development of novel therapies for tuberculosis and other challenging bacterial infections, contributing to the fight against antimicrobial resistance.

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Everything You Need To Know

What is the function of RimP in bacteria?

RimP, or Ribosomal maturation factor P, functions as a vital helper molecule during the assembly of ribosomes in bacteria. Its primary role involves interacting with other ribosomal components, particularly the small ribosomal protein S12 (RpsL). This interaction, facilitated by a flexible linker region within RimP, is crucial for coordinating the assembly process and ensuring the proper formation of functional ribosomes. Without RimP, ribosome assembly would be significantly impaired, hindering the bacteria's ability to produce proteins necessary for survival.

What does the structure of RimP reveal about its function?

The crystal structure of RimP from Mycobacterium smegmatis reveals that it consists of two distinct domains connected by a flexible linker region. Each domain contributes to the overall function of RimP, but it's the linker region that's especially important. This linker facilitates the interaction with ribosomal protein S12 (RpsL), and specific residues within the linker are essential for effective binding. The unique arrangement and interaction between the two domains, along with the crucial linker region, enable RimP to play its role in ribosome assembly.

Why is the interaction between RimP and S12 (RpsL) so important?

The interaction between RimP and S12 (RpsL) is fundamental for ribosome assembly. RimP's linker region is specifically responsible for binding to RpsL, and this interaction is essential for the normal function of the ribosome. Disrupting this interaction, such as through mutations in the linker region, significantly reduces RimP's ability to bind to RpsL, thereby impairing ribosome assembly. This highlights the critical role of RimP-RpsL interaction in the overall process of protein synthesis in bacteria.

How could RimP be targeted to fight bacterial infections like tuberculosis?

Targeting RimP offers a potential strategy for developing new antibacterial drugs, particularly against infections like tuberculosis. By disrupting RimP's function, it may be possible to halt ribosome production in bacteria, thereby inhibiting their growth and ability to cause disease. Given the essential role of RimP in ribosome assembly, drugs designed to interfere with RimP's structure or its interaction with S12 (RpsL) could provide a novel approach to combatting bacterial infections. This is an attractive approach, especially when resistance to existing antibiotics are on the rise.

What happens when the linker region of RimP is mutated?

Mutations in the linker region of RimP significantly reduce its ability to bind to ribosomal protein S12 (RpsL). Because of the linker's involvement in the interaction, the normal function of the ribosome will be affected. This demonstrates the critical role this linker plays in coordinating the interaction of RimP and S12 in Mycobacterium smegmatis, similar to that of Mycobacterium tuberculosis.