Balasubrahmanyam Addepalli

Mr. Balasubrahmanyam Addepalli

American Chemical Society (ACS-USA)
+2
orcid

Research Focus & Metrics

Academic Career Length

30Years (1997-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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1 June 2019 in Journal of Chromatography A
Verified
Journal Article
Closed access
PLPeter A. Lobue
Peter A. Lobue
MJManasses Jora
Manasses Jora
BABalasubrahmanyam Addepalli
Balasubrahmanyam Addepalli
PLPatrick Limbach
Patrick Limbach

1 January 2008 in BMC Genomics
Verified
Journal Article
Open access
PDF file
AHArthur G. Hunt
Arthur G. Hunt
RXRuqiang Xu
Ruqiang Xu
BABalasubrahmanyam Addepalli
Balasubrahmanyam Addepalli
SRSuryadevara Rao
Suryadevara Rao
KFKevin P Forbes
Kevin P Forbes
QLQingshun Quinn Li
Qingshun Quinn Li
The polyadenylation of mRNA is one of the critical processing steps during expression of almost all eukaryotic genes. It is tightly integrated with transcription, particularly its termination, as well as other RNA processing events, i.e. capping and splicing. The poly(A) tail protects the mRNA from unregulated degradation, and it is required for nuclear export and translation initiation. In recent years, it has been demonstrated that the polyadenylation process is also involved in the regulation of gene expression. The polyadenylation process requires two components, the cis-elements on the mRNA and a group of protein factors that recognize the cis-elements and produce the poly(A) tail. Here we report a comprehensive pairwise protein-protein interaction mapping and gene expression profiling of the mRNA polyadenylation protein machinery in Arabidopsis.

11 June 2008 in PLOS ONE
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Journal Article
Open access
PDF file
JZJingxian Zhang
Jingxian Zhang
BABalasubrahmanyam Addepalli
Balasubrahmanyam Addepalli
KYKil-Young Yun
Kil-Young Yun
AHArthur G. Hunt
Arthur G. Hunt
RXRuqiang Xu
Ruqiang Xu
DFDeane L. Falcone
Deane L. Falcone
Plants respond to many unfavorable environmental conditions via signaling mediated by altered levels of various reactive oxygen species (ROS). To gain additional insight into oxidative signaling responses, Arabidopsis mutants that exhibited tolerance to oxidative stress were isolated. We describe herein the isolation and characterization of one such mutant, oxt6. The oxt6 mutation is due to the disruption of a complex gene (At1g30460) that encodes the Arabidopsis ortholog of the 30-kD subunit of the cleavage and polyadenylation specificity factor (CPSF30) as well as a larger, related 65-kD protein. Expression of mRNAs encoding Arabidopsis CPSF30 alone was able to restore wild-type growth and stress susceptibility to the oxt6 mutant. Transcriptional profiling and single gene expression studies show elevated constitutive expression of a subset of genes that encode proteins containing thioredoxin- and glutaredoxin- related domains in the oxt6 mutant, suggesting that stress can be ameliorated by these gene classes. Bulk poly(A) tail length was not seemingly affected in the oxt6 mutant, but poly(A) site selection was different, indicating a subtle effect on polyadenylation in the mutant. These results implicate the Arabidopsis CPSF30 protein in the posttranscriptional control of the responses of plants to stress, and in particular to the expression of a set of genes that suffices to confer tolerance to oxidative stress.

1 March 2019 in Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms
Verified
Journal Article
Closed access
MJManasses Jora
Manasses Jora
PLPeter A. Lobue
Peter A. Lobue
RRRobert Ross
Robert Ross
BWBrittney Williams
Brittney Williams
BABalasubrahmanyam Addepalli
Balasubrahmanyam Addepalli

18 June 2007 in Nucleic Acids Research
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Journal Article
Open access
PDF file
BABalasubrahmanyam Addepalli
Balasubrahmanyam Addepalli
AHArthur G. Hunt
Arthur G. Hunt
The polyadenylation of messenger RNAs is mediated by a multi-subunit complex that is conserved in eukaryotes. Among the most interesting of these proteins is the 30-kDa-subunit of the Cleavage and Polyadenylation Specificity Factor, or CPSF30. In this study, the Arabidopsis CPSF30 ortholog, AtCPSF30, is characterized. This protein possesses an unexpected endonucleolytic activity that is apparent as an ability to nick and degrade linear as well as circular single-stranded RNA. Endonucleolytic action by AtCPSF30 leaves RNA 3′ ends with hydroxyl groups, as they can be labeled by RNA ligase with [32P]-cytidine-3′,5′-bisphosphate. Mutations in the first of the three CCCH zinc finger motifs of the protein abolish RNA binding by AtCPSF30 but have no discernible effects on nuclease activity. In contrast, mutations in the third zinc finger motif eliminate the nuclease activity of the protein, and have a modest effect on RNA binding. The N-terminal domain of another Arabidopsis polyadenylation factor subunit, AtFip1(V), dramatically inhibits the nuclease activity of AtCPSF30 but has a slight negative effect on the RNA-binding activity of the protein. These results indicate that AtCPSF30 is a probable processing endonuclease, and that its action is coordinated through its interaction with Fip1.

12 June 2018 in Journal of the American Society for Mass Spectrometry
Verified
Journal Article
Open access
PDF file
MJManasses Jora
Manasses Jora
ABAndrew P. Burns
Andrew P. Burns
RRRobert Ross
Robert Ross
PLPeter A. Lobue
Peter A. Lobue
RZRuoxia Zhao
Ruoxia Zhao
PLPatrick Limbach
Patrick Limbach
The analytical identification of positional isomers (e.g., 3-, N4-, 5-methylcytidine) within the > 160 different post-transcriptional modifications found in RNA can be challenging. Conventional liquid chromatography coupled with tandem mass spectrometry (LC-MS/MS) approaches rely on chromatographic separation for accurate identification because the collision-induced dissociation (CID) mass spectra of these isomers nearly exclusively yield identical nucleobase ions (BH2+) from the same molecular ion (MH+). Here, we have explored higher-energy collisional dissociation (HCD) as an alternative fragmentation technique to generate more informative product ions that can be used to differentiate positional isomers. LC-MS/MS of modified nucleosides characterized using HCD led to the creation of structure- and HCD energy-specific fragmentation patterns that generated unique fingerprints, which can be used to identify individual positional isomers even when they cannot be separated chromatographically. While particularly useful for identifying positional isomers, the fingerprinting capabilities enabled by HCD also offer the potential to generate HPLC-independent spectral libraries for the rapid analysis of modified ribonucleosides.