Uracil DNA-glycosylase/glyceraldehyde-3-phosphate dehydrogenase is an Ap4A binding protein

Baxi, Mayur D.; Vishwanatha, Jamboor K.

doi:10.1021/bi00030a007

Cited by 98 publications

(64 citation statements)

References 56 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Each 335-amino acid polypeptide contains two domains: an NAD ϩ binding/Rossmann-fold domain (residues 1-150 and 317-335) and a catalytic domain (residues 151-316). GAPDH is a multifunctional enzyme implicated in a variety of cellular processes including nucleic acid binding (13,(15)(16)(17)(18)(19), DNA replication and repair (20), nuclear tRNA transport (18), apoptosis (21,22), microtubule bundling (23), membrane fusion (24), neurodegenerative disorders (25,26), and heme incorporation (27). The mechanism by which GAPDH switches among these various functions in the cell is unknown but may depend on the cell status and GAPDH posttranslational modifications (for reviews, see Refs.…”

mentioning

confidence: 99%

A Dimer Interface Mutation in Glyceraldehyde-3-Phosphate Dehydrogenase Regulates Its Binding to AU-rich RNA

White

Khan

Deredge

et al. 2015

Journal of Biological Chemistry

View full text Add to dashboard Cite

Background:The glycolytic enzyme GAPDH is a non-canonical RNA-binding protein.Results: A dimer interface mutation impairs the two-step binding of GAPDH to AU-rich elements from TNF-␣ mRNA and leads to RNA structural changes. Conclusion: Dimer and tetramer interface residues are important for GAPDH-RNA binding. Significance: We propose a novel model for GAPDH binding to AU-rich RNA via the oligomeric interfaces.

show abstract

mentioning

confidence: 99%

A Dimer Interface Mutation in Glyceraldehyde-3-Phosphate Dehydrogenase Regulates Its Binding to AU-rich RNA

White

Khan

Deredge

et al. 2015

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…These include DNA repair (23,37,38); DNA, mRNA, and protein binding (39 -41); a possible role in RNA export (42); translational control (43); protein kinase activity (44); interactions with microtubules (45); and interactions with cell membranes (46). While these activities were reported mainly in mammalian GAPDH, such roles for the GAPDH protein in lower eukaryotes cannot be ruled out a priori considering the high degree of sequence conservation of GAPDH among these organisms.…”

Section: Discussionmentioning

confidence: 99%

Glyceraldehyde-3-phosphate Dehydrogenase Is Regulated on a Daily Basis by the Circadian Clock

Shinohara

Loros

Dunlap

1998

Journal of Biological Chemistry

View full text Add to dashboard Cite

Circadian clocks function to govern a wide range of rhythmic activities in organisms. An integral part of rhythmicity is the daily control of target genes by the clock. Here we describe the sequence and analysis of a novel clock-controlled gene, ccg-7, showing similarity to glyceraldehyde-3-phosphate dehydrogenase (GAPDH), a glycolytic enzyme widely used as a constitutive control in a variety of systems. That ccg-7 encodes GAPDH was confirmed by demonstrating that in vitro synthesized CCG-7 possesses GAPDH activity. Rhythms in both ccg-7 mRNA accumulation and CCG-7 (GAPDH) activity are observed in a clock wild-type strain where the peak in GAPDH activity lags several hours behind the peak in ccg-7 mRNA accumulation in the late night. Together with our previous observation that ccg-7 mRNA is not developmentally regulated, we show that ccg-7 is not induced by environmental stresses such as glucose or nitrogen deprivation (which also trigger development), heat shock, or osmotic stress. Thus, the finding that GAPDH is clock-regulated points to a specific role for the circadian clock in controlling aspects of general metabolism and provides evidence for circadian regulation of a gene found in most living organisms.

show abstract

“…Evidence is emerging that GAPDH is also involved in various other cellular functions, such as DNA binding (39,52), tRNA export (45), uracil DNA glycosylase activity (3,32), and association with polyribosomes (42). Furthermore, an RNA-unwinding property has been identified in GAPDH which is believed to facilitate translation of mRNAs in the polyribosomes (23).…”

mentioning

confidence: 99%

Specific Phosphorylated Forms of Glyceraldehyde 3-Phosphate Dehydrogenase Associate with Human Parainfluenza Virus Type 3 and Inhibit Viral Transcription In Vitro

Choudhary

Banerjee

2000

J Virol

View full text Add to dashboard Cite

). To gain further insight into these molecular interactions, we analyzed the virion-associated GAPDH and La protein using two-dimensional gel electrophoresis and immunoblotting. The GAPDH was resolved into two major and one minor molecular species migrating in the pI range of 7.6 to 8.3, while the La protein was resolved into five molecular species in the pI range of 6.8 to 7.5. The GAPDH isoforms present in the virions were also detected in the cytoplasmic fraction of CV-1 cell extract, albeit as minor species. On the other hand, the multiple molecular forms of La protein as seen within the virions were readily detected in the total CV-1 cell extract. Further analysis of virion-associated GAPDH by in vivo labeling with [ 32 P]orthophosphate revealed the presence of multiple phosphorylated species. The phosphorylated species were able to bind specifically to the viral cis-acting 3 genome sense RNA but failed to bind to the leader sense RNA, as determined by gel mobility shift assay. In contrast, the La protein isoforms present within the virions were not phosphorylated and bound to the viral cis-acting RNAs in a phosphorylation-independent manner. The GAPDH isoforms purified from the CV-1 cell cytoplasmic fraction inhibited viral transcription in vitro. Consistent with this, flag-tagged recombinant GAPDH synthesized by using the vaccinia virus expression system also inhibited viral transcription. Together, these data indicate that specific phosphorylated forms of GAPDH associate with HPIV3 and are involved in the regulation of virus gene expression.Human parainfluenza virus type 3 (HPIV3), a paramyxovirus, is second only to respiratory syncytial virus in causing severe respiratory tract infections in children and young adults (6). The single-stranded RNA genome of HPIV3, 15,461 nucleotides (nt) long, is contained within a helical nucleocapsid (15). Three virus-encoded proteins, the nucleocapsid protein N (68 kDa), the phosphoprotein P (90 kDa), and the RNA polymerase L (257 kDa), are associated with the nucleocapsid to form a transcribing ribonucleoprotein (RNP) complex (1, 15). The N protein enwraps the genome RNA, while the L and P proteins together constitute the RNA-dependent RNA polymerase complex that transcribes and replicates the N-bound genome RNA. During transcription, the RNA polymerase synthesizes a short leader RNA, followed by six capped and polyadenylated mRNAs. During replication, on the other hand, a full-length plus-strand copy of the genome RNA is synthesized which, in turn, serves as the template for synthesis of the minus-strand genome RNA (1, 6, 15). Studies from our laboratory, as well as others, indicate that cellular cytoskeletal proteins such as actin and tubulin are involved in the activation of transcription of several paramyxoviruses (4,9,12,22,34,35). Similarly, cellular RNA binding proteins that interact with the viral cis-acting elements are believed to be involved in the regulation of transcription and replication (25,26,28).The minus-sense genomic 3Ј end and its complementary l...

show abstract

Uracil DNA-glycosylase/glyceraldehyde-3-phosphate dehydrogenase is an Ap4A binding protein

Cited by 98 publications

References 56 publications

A Dimer Interface Mutation in Glyceraldehyde-3-Phosphate Dehydrogenase Regulates Its Binding to AU-rich RNA

A Dimer Interface Mutation in Glyceraldehyde-3-Phosphate Dehydrogenase Regulates Its Binding to AU-rich RNA

Glyceraldehyde-3-phosphate Dehydrogenase Is Regulated on a Daily Basis by the Circadian Clock

Specific Phosphorylated Forms of Glyceraldehyde 3-Phosphate Dehydrogenase Associate with Human Parainfluenza Virus Type 3 and Inhibit Viral Transcription In Vitro

Contact Info

Product

Resources

About