Comparison of the three-dimensional structures of human, yeast, and oat ubiquitin.

Vijay‐Kumar, Senadhi; Bugg, Charles E.; Wilkinson, Keith D.; Vierstra, Richard D.; Hatfield, Peggy M.; Cook, William J.

doi:10.1016/s0021-9258(18)45583-4

Cited by 140 publications

(41 citation statements)

References 13 publications

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“…Ub-like proteins have also been identified in prokaryotes, providing clues on the origin of this ubiquitous protein [ 2 ]. The structure of Ub revealed a unique fold formed by a β-sheet with five antiparallel β-strands and a single helical segment, which is shared by other Ub-like proteins and domains, known as the β-grasp fold ( Figure 1 ) [ 1 , 3 ].…”

Section: Introductionmentioning

confidence: 99%

Ubiquitin and Ubiquitin-Like Proteins and Domains in Ribosome Production and Function: Chance or Necessity?

Martín-Villanueva

Gutiérrez

Kressler

et al. 2021

IJMS

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Ubiquitin is a small protein that is highly conserved throughout eukaryotes. It operates as a reversible post-translational modifier through a process known as ubiquitination, which involves the addition of one or several ubiquitin moieties to a substrate protein. These modifications mark proteins for proteasome-dependent degradation or alter their localization or activity in a variety of cellular processes. In most eukaryotes, ubiquitin is generated by the proteolytic cleavage of precursor proteins in which it is fused either to itself, constituting a polyubiquitin precursor, or as a single N-terminal moiety to ribosomal proteins, which are practically invariably eL40 and eS31. Herein, we summarize the contribution of the ubiquitin moiety within precursors of ribosomal proteins to ribosome biogenesis and function and discuss the biological relevance of having maintained the explicit fusion to eL40 and eS31 during evolution. There are other ubiquitin-like proteins, which also work as post-translational modifiers, among them the small ubiquitin-like modifier (SUMO). Both ubiquitin and SUMO are able to modify ribosome assembly factors and ribosomal proteins to regulate ribosome biogenesis and function. Strikingly, ubiquitin-like domains are also found within two ribosome assembly factors; hence, the functional role of these proteins will also be highlighted.

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Section: Introductionmentioning

confidence: 99%

Ubiquitin and Ubiquitin-Like Proteins and Domains in Ribosome Production and Function: Chance or Necessity?

Martín-Villanueva

Gutiérrez

Kressler

et al. 2021

IJMS

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“…Basic aa 26, 27, 30, and 32 were proposed to be involved in MA binding to phospholipids ( 13 , 99 , 101 ). F , human ubiquitin X-ray structure (PDB entry 1UBQ ) ( 135 ), showing that the hydrophobic patch in MA consisting of Leu-31, Val-35, and Trp-36 resembles the hydrophobic ubiquitin patch consisting of Leu-8, Ile-44, and Val-70 which is involved in ubiquitin binding to Vps23, Bro1, TSG101, and ALIX ( 58 , 67 , 102 ). G , Bro1 coimmunoprecipitation with GFP-tagged CA versions, showing that Bro1 binds to the N-terminal CA domain; same as B except that GFP-tagged CA, NCA (aa 133–278), or CCA (aa 279–363) was expressed in a yeast strain carrying genomically 3HA-tagged Bro1 and that coimmunoprecipitated Bro1 was detected by immunoblotting with anti-HA antibodies.…”

Section: Resultsmentioning

confidence: 99%

HIV-1 Gag release from yeast reveals ESCRT interaction with the Gag N-terminal protein region

Meusser

Purfuerst

Luft

2020

Journal of Biological Chemistry

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The HIV-1 protein Gag assembles at the plasma membrane and drives virion budding, assisted by the cellular endosomal-complex-required-for-transport (ESCRT) proteins. Two ESCRT proteins, TSG101 and ALIX, bind to the Gag C-terminal p6 peptide. TSG101 binding is important for efficient HIV-1 release, but how ESCRTs contribute to the budding process and how their activity is coordinated with Gag assembly is poorly understood. Yeast, allowing genetic manipulation that is not easily available in human cells, has been used to characterize the cellular ESCRT function. Previous work reported Gag budding from yeast spheroplasts, but Gag release was ESCRT independent. We developed a yeast model for ESCRT-dependent Gag release. We combined yeast genetics and Gag mutational analysis with Gag-ESCRT binding studies and the characterization of Gag-plasma-membrane binding and Gag release. With our system, we identified a previously unknown interaction between ESCRT proteins and the Gag N-terminal protein region. Mutations in the Gag plasma-membrane-binding matrix domain that reduced Gag-ESCRT binding increased Gag-plasma-membrane binding and Gag release. ESCRT knockout mutants showed that the release enhancement was an ESCRT-dependent effect. Similarly, matrix mutation enhanced Gag release from human HEK293 cells. Release enhancement partly depended on ALIX binding to p6, although binding-site mutation did not impair WT Gag release. Accordingly, the relative affinity for matrix compared to p6 in GST-pull-down experiments was higher for ALIX than for TSG101. We suggest that a transient matrix-ESCRT interaction is replaced when Gag binds to the plasma membrane. This step may activate ESCRT proteins and thereby coordinate ESCRT function with virion assembly.

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“…This PMT consists of intracellular protein modification by adding one or more ubiquitin (Ub) protein(s) (for a review see [119]). Ub is a 76-amino acid polypeptide, which has a conserved structure [120]. The Ub sequence contains seven K residues that can be used for subsequent Ub linkage leading to polyubiquitination (for a review see [121]), even if the two most common polyubiquitination chains consist in the formation of Ub chain connected to residues K48 or K63 of Ub.…”

Section: Hiv-1 Pr55 Gag Ubiquitinationmentioning

confidence: 99%

Post-Translational Modifications of Retroviral HIV-1 Gag Precursors: An Overview of Their Biological Role

Bussienne

Marquet

Paillart

et al. 2021

IJMS

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Protein post-translational modifications (PTMs) play key roles in eukaryotes since they finely regulate numerous mechanisms used to diversify the protein functions and to modulate their signaling networks. Besides, these chemical modifications also take part in the viral hijacking of the host, and also contribute to the cellular response to viral infections. All domains of the human immunodeficiency virus type 1 (HIV-1) Gag precursor of 55-kDa (Pr55Gag), which is the central actor for viral RNA specific recruitment and genome packaging, are post-translationally modified. In this review, we summarize the current knowledge about HIV-1 Pr55Gag PTMs such as myristoylation, phosphorylation, ubiquitination, sumoylation, methylation, and ISGylation in order to figure out how these modifications affect the precursor functions and viral replication. Indeed, in HIV-1, PTMs regulate the precursor trafficking between cell compartments and its anchoring at the plasma membrane, where viral assembly occurs. Interestingly, PTMs also allow Pr55Gag to hijack the cell machinery to achieve viral budding as they drive recognition between viral proteins or cellular components such as the ESCRT machinery. Finally, we will describe and compare PTMs of several other retroviral Gag proteins to give a global overview of their role in the retroviral life cycle.

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Comparison of the three-dimensional structures of human, yeast, and oat ubiquitin.

Cited by 140 publications

References 13 publications

Ubiquitin and Ubiquitin-Like Proteins and Domains in Ribosome Production and Function: Chance or Necessity?

Ubiquitin and Ubiquitin-Like Proteins and Domains in Ribosome Production and Function: Chance or Necessity?

HIV-1 Gag release from yeast reveals ESCRT interaction with the Gag N-terminal protein region

Post-Translational Modifications of Retroviral HIV-1 Gag Precursors: An Overview of Their Biological Role

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