Structurally conserved and functionally divergent yeast Ssu72 phosphatases

Related Experiment Video

Updated: May 10, 2026

Enzymatic Modification and Flow Cytometry Assessment of Yeast Surface Displayed Proteins
10:54

Enzymatic Modification and Flow Cytometry Assessment of Yeast Surface Displayed Proteins

Published on: May 30, 2025

Ana M Rodríguez-Torres1, Mónica Lamas-Maceiras, Rosa García-Díaz

  • 1Area de Bioquímica, Facultad de Ciencias, Universidade da Coruña (UDC), A Coruña, Spain.

FEBS Letters
|July 9, 2013
PubMed

Keywords:
5-fluoro-orotic acidCTDCTD-phosphataseFOAGSTOD(600)RNA polymerase IIRNA polymerase-IIRNA-processingRNAPIISSU72Ser2, Ser5Yeastcarboxy-terminal domain (CTD) of the major subunit of RNA polymerase IIglutathione S-transferaseoptical density at 600 nanometerspNPPparanitrophenylphosphateserine 2 and 5, respectively, from CTD repeats

More Related Videos

Budding Yeast Protein Extraction and Purification for the Study of Function, Interactions, and Post-translational Modifications09:22

Budding Yeast Protein Extraction and Purification for the Study of Function, Interactions, and Post-translational Modifications

Published on: October 30, 2013

Applications of pHluorin for Quantitative, Kinetic and High-throughput Analysis of Endocytosis in Budding Yeast10:02

Applications of pHluorin for Quantitative, Kinetic and High-throughput Analysis of Endocytosis in Budding Yeast

Published on: October 23, 2016

Related Concept Videos

Septins01:19

Septins

Septins are protein filaments forming the cytoskeleton along with the microtubules, microfilaments, intermediate filaments, and other accessory proteins. In 1971 while studying the cell division cycle in mutant Saccharomyces cerevisiae Harwell et al. first identified the septin-related genes playing a crucial role in yeast cytokinesis. Fluorescence microscopy revealed that these proteins localize at the budding neck as rings. These ring-like proteins were then named Septins by John Pringle, and...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Overview of Secretory Vesicles01:33

Overview of Secretory Vesicles

Secretory vesicles, also known as dense core vesicles (DCVs), are membrane-bound vesicles that transport secretory proteins, such as hormones or neurotransmitters. Regulated secretory vesicles transport proteins from the trans-Golgi network to the exterior of the cell. Proteins present in regulated secretory vesicles are required to be rapidly exocytosed in large amounts upon a specific stimulus.
Various proteins regulate the aggregation of molecules inside the secretory vesicles. Chromogranins...
Covalently Linked Protein Regulators02:04

Covalently 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.