Cement precursor proteins of the reef-building polychaete Phragmatopoma californica (Fewkes)

Biochemistry ◽  
1992 ◽  
Vol 31 (25) ◽  
pp. 5733-5738 ◽  
Author(s):  
J. Herbert Waite ◽  
Rebecca A. Jensen ◽  
Daniel E. Morse
Keyword(s):  
Precursor Proteins ◽  
Phragmatopoma Californica

Structure of contact sites between the outer and inner mitochondrial membranes investigated by HVEM tomography

1996 ◽  
Vol 54 ◽  
pp. 966-967
Author(s):  
C.A. Mannella ◽  
K.F. Buttle ◽  
K.A. O‘Farrell ◽  
A. Leith ◽  
M. Marko
Keyword(s):  
Liver Mitochondrion ◽  
Adenine Nucleotide ◽  
Protein Complexes ◽  
Mitochondrial Membranes ◽  
Electron Microscopic ◽  
Contact Sites ◽  
Transmission Electron ◽  
Precursor Proteins ◽  
Membrane Contacts ◽  
And Function

Early transmission electron microscopy of plastic-embedded, thin-sectioned mitochondria indicated that there are numerous junctions between the outer and inner membranes of this organelle. More recent studies have suggested that the mitochondrial membrane contacts may be the site of protein complexes engaged in specialized functions, e.g., import of mitochondrial precursor proteins, adenine nucleotide channeling, and even intermembrane signalling. It has been suggested that the intermembrane contacts may be sites of membrane fusion involving non-bilayer lipid domains in the two membranes. However, despite growing interest in the nature and function of intramitochondrial contact sites, little is known about their structure.We are using electron microscopic tomography with the Albany HVEM to determine the internal organization of mitochondria. We have reconstructed a 0.6-μm section through an isolated, plasticembedded rat-liver mitochondrion by combining 123 projections collected by tilting (+/- 70°) around two perpendicular tilt axes. The resulting 3-D image has confirmed the basic inner-membrane organization inferred from lower-resolution reconstructions obtained from single-axis tomography.

scholarly journals Vacuolar ATPase mutants accumulate precursor proteins in a pre-vacuolar compartment

1993 ◽  
Vol 268 (14) ◽  
pp. 10564-10572
Author(s):  
D.S. Yaver ◽  
H. Nelson ◽  
N. Nelson ◽  
D.J. Klionsky
Keyword(s):  
Vacuolar Atpase ◽  
Vacuolar Compartment ◽  
Precursor Proteins

scholarly journals Energy requirements for unfolding and membrane translocation of precursor proteins during import into mitochondria.

1990 ◽  
Vol 265 (27) ◽  
pp. 16324-16329 ◽  
Author(s):  
N Pfanner ◽  
J Rassow ◽  
B Guiard ◽  
T Söllner ◽  
F U Hartl ◽  
...  
Keyword(s):  
Energy Requirements ◽  
Membrane Translocation ◽  
Precursor Proteins

scholarly journals Identification of Low Molecular Weight Proteins and Peptides from Schistosoma mekongi Worm, Egg and Infected Mouse Sera

Biomolecules ◽  
2021 ◽  
Vol 11 (4) ◽  
pp. 559
Author(s):  
Tipparat Thiangtrongjit ◽  
Nattapon Simanon ◽  
Poom Adisakwattana ◽  
Yanin Limpanont ◽  
Phiraphol Chusongsang ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Infected Mouse ◽  
In Silico ◽  
Limited Information ◽  
Schistosoma Mekongi ◽  
River Region ◽  
Precursor Proteins ◽  
Peptide Profiles ◽  
Low Sensitivity ◽  
Proteins And Peptides

Schistosoma mekongi is found in the lower Mekong river region and causes schistosomiasis. Low sensitivity of diagnosis and development of drug resistance are problems to eliminate this disease. To develop novel therapies and diagnostics for S. mekongi, the basic molecular biology of this pathogen needs to be explored. Bioactive peptides have been reported in several worms and play important roles in biological functions. Limited information is available on the S. mekongi peptidome. Therefore, this study aimed to identify S. mekongi peptides using in silico transcriptome mining and mass spectrometry approaches. Schistosoma peptide components were identified in adult worms, eggs, and infected mouse sera. Thirteen neuropeptide families were identified using in silico predictions from in-house transcriptomic databases of adult S. mekongi worms. Using mass spectrometry approaches, 118 peptides (from 54 precursor proteins) and 194 peptides (from 86 precursor proteins) were identified from adult worms and eggs, respectively. Importantly, eight unique peptides of the S. mekongi ubiquitin thioesterase, trabid, were identified in infected mouse sera 14, 28, and 56 days after infection. This protein may be a potential target for diagnosis of schistosomiasis. The S. mekongi peptide profiles determined in this study could be used for further drug and diagnostic development.

scholarly journals Uncleaved signals for glycosylphosphatidylinositol anchoring cause retention of precursor proteins in the endoplasmic reticulum

1993 ◽  
Vol 268 (16) ◽  
pp. 12017-12027
Author(s):  
M.D. Delahunty ◽  
F.J. Stafford ◽  
L.C. Yuan ◽  
D. Shaz ◽  
J.S. Bonifacino
Keyword(s):  
Endoplasmic Reticulum ◽  
Precursor Proteins

scholarly journals ATP Is Required for the Binding of Precursor Proteins to Chloroplasts

1989 ◽  
Vol 264 (12) ◽  
pp. 6724-6729 ◽  
Author(s):  
L J Olsen ◽  
S M Theg ◽  
B R Selman ◽  
K Keegstra
Keyword(s):  
Precursor Proteins

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

2021 ◽  
Vol 22 (9) ◽  
pp. 4359
Author(s):  
Sara Martín-Villanueva ◽  
Gabriel Gutiérrez ◽  
Dieter Kressler ◽  
Jesús de la Cruz
Keyword(s):  
Ribosomal Proteins ◽  
Ribosome Biogenesis ◽  
Ribosome Assembly ◽  
Cellular Processes ◽  
Substrate Protein ◽  
Precursor Proteins ◽  
Assembly Factors ◽  
Ubiquitin Moiety ◽  
And Function

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.

Identification of folding preferences of cleavage junctions of HIV-1 precursor proteins for regulation of cleavability

2010 ◽  
Vol 17 (2) ◽  
pp. 391-399 ◽  
Author(s):  
Hirotaka Ode ◽  
Masaru Yokoyama ◽  
Tadahito Kanda ◽  
Hironori Sato
Keyword(s):  
Precursor Proteins ◽  
Hiv 1
Sign in / Sign up

Export Citation Format

Share Document