Related Concept Videos
01:26Protein Modifications in the RER
Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
02:04Covalently Linked Protein Regulators
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
These groups modify specific amino acids in a protein.
01:41The Supercomplexes in the Crista Membrane
The mitochondrial cristae membrane is the primary site for the oxidative phosphorylation (OXPHOS) process of energy conversion mediated through respiratory complexes I to V. These complexes have been widely studied for decades, and it has been proven that they form supramolecular structures called respiratory supercomplexes (SC). These higher-order complexes may be crucial in maintaining the biochemical structure and improving the physiological activity of the individual complexes while...
01:20Sulfur Assimilation
Sulfur is an essential element in biological systems, contributing to synthesizing key biomolecules, including amino acids such as cysteine and methionine, and cofactors such as coenzyme A and biotin. Microorganisms primarily assimilate sulfur as sulfate (SO₄²⁻) from the environment, which must undergo a series of biochemical transformations before it can be incorporated into cellular components. As sulfate is highly oxidized, it must undergo assimilatory sulfate reduction to become...
01:49Conserved Binding Sites
Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
02:53Ribosomal RNA Synthesis
Ribosome synthesis is a highly complex and coordinated process involving more than 200 assembly factors. The synthesis and processing of ribosomal components occurs not only in the nucleolus but also in the nucleoplasm and the cytoplasm of eukaryotic cells.
Ribosome biogenesis begins with the synthesis of 5S and 45S pre-rRNAs by distinct RNA polymerases. The primary transcripts are extensively processed and modified before they are bound and folded by ribosomal proteins and assembly factors,...
Ribosome biogenesis begins with the synthesis of 5S and 45S pre-rRNAs by distinct RNA polymerases. The primary transcripts are extensively processed and modified before they are bound and folded by ribosomal proteins and assembly factors,...
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Iron-sulphur clusters in nucleic acid processing enzymes.
Malcolm F White1, Mark S Dillingham
1Biomedical Sciences Research Complex, University of St Andrews, North Haugh, St Andrews, Fife KY16 9ST, UK. mfw2@st-andrews.ac.uk
Current Opinion in Structural Biology
|December 16, 2011
Summary
Iron-sulfur clusters are increasingly found in nucleic acid processing proteins. This review explores their diverse roles and potential common mechanisms in enzymes like RNA polymerases and helicases.
Area of Science:
- Biochemistry
- Molecular Biology
- Structural Biology
Background:
- Iron-sulfur clusters were once considered rare in nucleic acid binding proteins.
- Recent literature reveals their essential role in diverse nucleic acid processing machinery.
Purpose of the Study:
- To review recent developments concerning iron-sulfur clusters in nucleic acid enzymes.
- To discuss potential common mechanistic roles for these clusters.
Main Methods:
- Literature review of recent findings.
- Analysis of crystal structures of iron-sulfur enzymes.
- Discussion of mechanistic roles.
Main Results:
- Iron-sulfur clusters are components of glycosylases, primases, helicases, nucleases, transcription factors, RNA polymerases, and RNA methyltransferases.
- The precise function of these clusters is often poorly understood.
- Crystal structures show limited commonalities among these iron-sulfur enzymes.
Conclusions:
- Iron-sulfur clusters play crucial, though often uncharacterized, roles in nucleic acid processing.
- Further research is needed to elucidate common mechanistic principles governing their function across different enzymes.