scholarly journals ERS-24, a Mammalian v-SNARE Implicated in Vesicle Traffic between the ER and the Golgi

1997 ◽  
Vol 137 (5) ◽  
pp. 1017-1028 ◽  
Author(s):  
Inbok Paek ◽  
Lelio Orci ◽  
Mariella Ravazzola ◽  
Hediye Erdjument-Bromage ◽  
Mylene Amherdt ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Endoplasmic Reticulum ◽  
Sequence Homology ◽  
Vesicular Transport ◽  
Dependent Manner ◽  
Vesicle Traffic ◽  
Transport Vesicles ◽  
Identification And Characterization

We report the identification and characterization of ERS-24 (Endoplasmic Reticulum SNARE of 24 kD), a new mammalian v-SNARE implicated in vesicular transport between the ER and the Golgi. ERS24 is incorporated into 20S docking and fusion particles and disassembles from this complex in an ATP-dependent manner. ERS-24 has significant sequence homology to Sec22p, a v-SNARE in Saccharomyces cerevisiae required for transport between the ER and the Golgi. ERS-24 is localized to the ER and to the Golgi, and it is enriched in transport vesicles associated with these organelles.

scholarly journals Yos1p Is a Novel Subunit of the Yip1p–Yif1p Complex and Is Required for Transport between the Endoplasmic Reticulum and the Golgi Complex

2005 ◽  
Vol 16 (4) ◽  
pp. 1673-1683 ◽  
Author(s):  
Matthew Heidtman ◽  
Catherine Z. Chen ◽  
Ruth N. Collins ◽  
Charles Barlowe
Keyword(s):  
Endoplasmic Reticulum ◽  
Golgi Complex ◽  
Secretory Pathway ◽  
Integral Membrane Protein ◽  
Rab Gtpases ◽  
Reading Frame ◽  
Multicopy Suppressor ◽  
Transport Vesicles ◽  
Identification And Characterization

Yeast Yip1p is a member of a conserved family of transmembrane proteins that interact with Rab GTPases. Previous studies also have indicated a role for Yip1p in the biogenesis of endoplasmic reticulum (ER)-derived COPII transport vesicles. In this report, we describe the identification and characterization of the uncharacterized open reading frame YER074W-A as a novel multicopy suppressor of the thermosensitive yip1-4 strain. We have termed this gene Yip One Suppressor 1 (YOS1). Yos1p is essential for growth and for function of the secretory pathway; depletion or inactivation of Yos1p blocks transport between the ER and the Golgi complex. YOS1 encodes an integral membrane protein of 87 amino acids that is conserved in eukaryotes. Yos1p localizes to ER and Golgi membranes and is efficiently packaged into ER-derived COPII transport vesicles. Yos1p associates with Yip1p and Yif1p, indicating Yos1p is a novel subunit of the Yip1p–Yif1p complex.

scholarly journals Identification and characterization of Fep15, a new selenocysteine-containing member of the Sep15 protein family

2006 ◽  
Vol 394 (3) ◽  
pp. 575-579 ◽  
Author(s):  
Sergey V. Novoselov ◽  
Deame Hua ◽  
Alexey V. Lobanov ◽  
Vadim N. Gladyshev
Keyword(s):  
Mammalian Cells ◽  
Insertion Sequence ◽  
Phylogenetic Analyses ◽  
Dependent Manner ◽  
Putative Active Site ◽  
A Genome ◽  
Sequence Elements ◽  
Identification And Characterization ◽  
Insertion Sequence Elements

Sec (selenocysteine) is a rare amino acid in proteins. It is co-translationally inserted into proteins at UGA codons with the help of SECIS (Sec insertion sequence) elements. A full set of selenoproteins within a genome, known as the selenoproteome, is highly variable in different organisms. However, most of the known eukaryotic selenoproteins are represented in the mammalian selenoproteome. In addition, many of these selenoproteins have cysteine orthologues. Here, we describe a new selenoprotein, designated Fep15, which is distantly related to members of the 15 kDa selenoprotein (Sep15) family. Fep15 is absent in mammals, can be detected only in fish and is present in these organisms only in the selenoprotein form. In contrast with other members of the Sep15 family, which contain a putative active site composed of Sec and cysteine, Fep15 has only Sec. When transiently expressed in mammalian cells, Fep15 incorporated Sec in an SECIS- and SBP2 (SECIS-binding protein 2)-dependent manner and was targeted to the endoplasmic reticulum by its N-terminal signal peptide. Phylogenetic analyses of Sep15 family members suggest that Fep15 evolved by gene duplication.

scholarly journals Identification and Characterization of OscR, a Transcriptional Regulator Involved in Osmolarity Adaptation in Vibrio cholerae

2009 ◽  
Vol 191 (13) ◽  
pp. 4082-4096 ◽  
Author(s):  
Nicholas J. Shikuma ◽  
Fitnat H. Yildiz
Keyword(s):  
Vibrio Cholerae ◽  
Biofilm Formation ◽  
Transcriptional Regulator ◽  
Dependent Manner ◽  
Genome Wide ◽  
Low Salt ◽  
Adaptation Response ◽  
Matrix Production ◽  
Identification And Characterization

ABSTRACT Vibrio cholerae is a facultative human pathogen. In its aquatic habitat and as it passes through the digestive tract, V. cholerae must cope with fluctuations in salinity. We analyzed the genome-wide transcriptional profile of V. cholerae grown at different NaCl concentrations and determined that the expression of compatible solute biosynthesis and transporter genes, virulence genes, and genes involved in adhesion and biofilm formation is differentially regulated. We determined that salinity modulates biofilm formation, and this response was mediated through the transcriptional regulators VpsR and VpsT. Additionally, a transcriptional regulator controlling an osmolarity adaptation response was identified. This regulator, OscR (osmolarity controlled regulator), was found to modulate the transcription of genes involved in biofilm matrix production and motility in a salinity-dependent manner. oscR mutants were less motile and exhibited enhanced biofilm formation only under low-salt conditions.

scholarly journals The Identification and Characterization of ADR6, a Gene Required for Sporulation and for Expression of the Alcohol Dehydrogenase II Isozyme From Saccharomyces cerevisiae

Genetics ◽  
1987 ◽  
Vol 116 (4) ◽  
pp. 523-530
Author(s):  
Aileen K W Taguchi ◽  
Elton T Young
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Alcohol Dehydrogenase ◽  
Isocitrate Lyase ◽  
Carbon Sources ◽  
Recessive Mutation ◽  
Yeast Saccharomyces Cerevisiae ◽  
Upstream Activating Sequence ◽  
Adh Activity ◽  
Identification And Characterization

ABSTRACT The alcohol dehydrogenase II isozyme (enzyme, ADHII; structural gene, ADH2) of the yeast, Saccharomyces cerevisiae, is under stringent carbon catabolite control. This cytoplasmic isozyme exhibits negligible activity during growth in media containing fermentable carbon sources such as glucose and is maximal during growth on nonfermentable carbon sources. A recessive mutation, adr6-1, and possibly two other alleles at this locus, were selected for their ability to decrease Ty-activated ADH2-6 c expression. The adr6-1 mutation led to decreased ADHII activity in both ADH2-6c and ADH2+ strains, and to decreased levels of ADH2 mRNA. Ty transcription and the expression of two other carbon catabolite regulated enzymes, isocitrate lyase and malate dehydrogenase, were unaffected by the adr6-1 mutation. adr6-1/adr6-1strains were defective for sporulation, indicating that adr6 mutations may have pleiotropic effects. The sporulation defect was not a consequence of decreased ADH activity. Since the ADH2-6c mutation is due to insertion of a 5.6-kb Ty element at the TATAA box, it appears that the ADR6+-dependent ADHII activity required ADH2 sequences 3′ to or including the TATAA box. The ADH2 upstream activating sequence (UAS) was probably not required. The ADR6 locus was unlinked to the ADR1 gene which encodes another trans-acting element required for ADH2 expression.

scholarly journals Identification and Characterization of Four Autophagy-Related Genes That Are Expressed in Response to Hypoxia in the Brain of the Oriental River Prawn (Macrobrachium nipponense)

2019 ◽  
Vol 20 (8) ◽  
pp. 1856 ◽  
Author(s):  
Shengming Sun ◽  
Ying Wu ◽  
Hongtuo Fu ◽  
Xianping Ge ◽  
Hongzheng You ◽  
...  
Keyword(s):  
Developmental Stages ◽  
Open Reading Frames ◽  
Dependent Manner ◽  
Macrobrachium Nipponense ◽  
Oriental River Prawn ◽  
Adverse Environmental Conditions ◽  
The Brain ◽  
Identification And Characterization

Autophagy is a cytoprotective mechanism triggered in response to adverse environmental conditions. Herein, we investigated the autophagy process in the oriental river prawn (Macrobrachium nipponense) following hypoxia. Full-length cDNAs encoding autophagy-related genes (ATGs) ATG3, ATG4B, ATG5, and ATG9A were cloned, and transcription following hypoxia was explored in different tissues and developmental stages. The ATG3, ATG4B, ATG5, and ATG9A cDNAs include open reading frames encoding proteins of 319, 264, 268, and 828 amino acids, respectively. The four M. nipponense proteins clustered separately from vertebrate homologs in phylogenetic analysis. All four mRNAs were expressed in various tissues, with highest levels in brain and hepatopancreas. Hypoxia up-regulated all four mRNAs in a time-dependent manner. Thus, these genes may contribute to autophagy-based responses against hypoxia in M. nipponense. Biochemical analysis revealed that hypoxia stimulated anaerobic metabolism in the brain tissue. Furthermore, in situ hybridization experiments revealed that ATG4B was mainly expressed in the secretory and astrocyte cells of the brain. Silencing of ATG4B down-regulated ATG8 and decreased cell viability in juvenile prawn brains following hypoxia. Thus, autophagy is an adaptive response protecting against hypoxia in M. nipponense and possibly other crustaceans. Recombinant MnATG4B could interact with recombinant MnATG8, but the GST protein could not bind to MnATG8. These findings provide us with a better understanding of the fundamental mechanisms of autophagy in prawns.

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