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Kumar, Abhishek

Spliceosomal Proteins Encoded by Fungal Genomes

Abstract Views :253 | PDF Views:70

Authors

Sandeep J. Sarde ¹, Frank Kempken ¹, Abhishek Kumar ²

Affiliations
1 Abteilung Botanische Genetik und Molekularbiologie, Botanisches Institut und Botanischer Garten, Christian-Albrechts-Universitat zu Kiel, Olshausenstr. 40 24098 Kiel, DE
2 Molecular Genetic Epidemiology (C050), German Cancer Research Center (DKFZ), Im Neuenheimer Feld 580 69120 Heidelberg, DE

Source

Current Science, Vol 114, No 08 (2018), Pagination: 1677-1686

Abstract

A large number of spliceosomal proteins are required for proper RNA splicing. While spliceosomal proteins from several model organisms have been analysed, only limited studies are available for fungal species. Hence, we have performed a comparative genomic analysis using eight fungal species belonging to three taxa (Ascomycetes, Basidiomycetes and Glomeromycota). We identified variable number of spliceosomal proteins in fungal species. From the small nuclear ribonucleoproteins (snRNPs), all the snRNPs were identified. In non-snRNPs, only some sub-groups were found extensively conserved in all fungal species, including PRP19 complex proteins, catalytic step II and late-acting proteins. In heterogeneous nuclear ribonucleoproteins (hnRNPs), variable number of proteins was identified. The number of spliceosomal proteins identified in filamentous fungi was higher than that in yeast. The collection of these spliceosomal proteins provides further insight into pre-mRNA splicing in fungi.

Keywords

Fungal Genomes, pre-mRNA, snRNPs, Spliceosomal Proteins.

Full Text

References

Brow, D. A., Allosteric cascade of spliceosome activation. Annu. Rev. Genet., 2002, 36, 333–360.

Irimia, M. and Roy, S. W., Origin of spliceosomal introns and alternative splicing. Cold Spring Harb. Perspect. Biol., 2014, 6.

Calarco, J. A., Zhen, M. and Blencowe, B. J., Networking in a global world: establishing functional connections between neural splicing regulators and their target transcripts. RNA, 2011, 17, 775–791.

Hoskins, A. A. and Moore, M. J., The spliceosome: a flexible, reversible macromolecular machine. Trends Biochem. Sci., 2012, 37, 179–188.

Ramani, A. K. et al., Genome-wide analysis of alternative splicing in Caenorhabditis elegans. Genome Res., 2011, 21, 342–348.

Will, C. L. and Luhrmann, R., Spliceosome structure and function. Cold Spring Harb. Perspect. Biol., 2011, 3.

Will, C. L. and Lührmann, R., The RNA World, Cold Spring Harbor Laboratory Press, New York, 2006.

Yu, B. et al., Spliceosomal genes in the D. discoideum genome: A comparison with those in H. sapiens, D. melanogaster, A. thaliana and S. cerevisiae. Protein Cell, 2011, 2, 395–409.

Beggs, J. D., Lsm proteins and RNA processing. Biochem. Soc. Trans., 2005, 33, 433–438.

He, W. and Parker, R., Functions of lsm proteins in mRNA degradation and splicing. Curr. Opin. Cell Biol., 2000, 12, 346–350.

Salgado-Garrido, J., Bragado-Nilsson, E., Kandels-Lewis, S. and Seraphin, B., Sm and Sm-like proteins assemble in two related complexes of deep evolutionary origin. EMBO. J., 1999, 18, 3451–3462.

Fromont-Racine, M., Rain, J. C. and Legrain, P., Toward a functional analysis of the yeast genome through exhaustive two-hybrid screens. Nat. Genet., 1997, 16, 277–282.

Klein Gunnewiek, J. M., Hussein, R. I., van Aarssen, Y., Palacios, D., de Jong, R., van Venrooij, W. J. and Gunderson, S. I., Fourteen residues of the U1 snRNP-specific U1a protein are required for homodimerization, cooperative RNA binding, and inhibition of polyadenylation. Mol. Cell Biol., 2000, 20, 2209–2217.

Aasland, R., Stewart, A. F. and Gibson, T., The SANT domain: a putative DNA-binding domain in the SWI-SNF and ADA complexes, the transcriptional co-repressor N-CoR and TFIIIB. Trends Biochem. Sci., 1996, 21, 87–88.

Chaudhury, A., Chander, P. and Howe, P. H., Heterogeneous nuclear ribonucleoproteins (hnrNPS) in cellular processes: focus on hnRNP E1’s multifunctional regulatory roles. RNA, 2010, 16, 1449–1462.

Dreyfuss, G., Matunis, M. J., Pinol-Roma, S. and Burd, C. G., hnRNP proteins and the biogenesis of mRNA. Annu. Rev. Biochem., 1993, 62, 289–321.

Mourelatos, Z., Abel, L., Yong, J., Kataoka, N. and Dreyfuss, G., Smn interacts with a novel family of hnRNP and spliceosomal proteins. Embo. J., 2001, 20, 5443–5452.

Miau, L. H., Chang, C. J., Shen, B. J., Tsai, W. H. and Lee, S. C., Identification of heterogeneous nuclear ribonucleoprotein K (hnRNP K) as a repressor of C/EBP -mediated gene activation. J. Biol. Chem., 1998, 273, 10784–10791.

Mayeda, A. and Krainer, A. R., Regulation of alternative pre-mRNA splicing by hnRNP A1 and splicing factor SF2. Cell, 1992, 68, 365–375.

Finn, R. D., Clements, J. and Eddy, S. R., HMMER web server: interactive sequence similarity searching. Nucleic Acids Res., 2011, 39, W29–W37.

Tamura, K., Peterson, D., Peterson, N., Stecher, G., Nei, M. and Kumar, S., MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods. Mol. Biol. Evol., 2011, 28, 2731–2739.

Pomeranz Krummel, D. A., Oubridge, C., Leung, A. K., Li, J. and Nagai, K., Crystal structure of human spliceosomal U1 snRNP at 5.5 a resolution. Nature, 2009, 458, 475–480.

Forch, P., Puig, O., Martinez, C., Seraphin, B. and Valcarcel, J., The splicing regulator TIA-1 interacts with U1-C to promote U1 snRNP recruitment to 5 splice sites. EMBO J., 2002, 21, 6882–6892.

Query, C. C., Bentley, R. C. and Keene, J. D., A common RNA recognition motif identified within a defined U1 RNA binding domain of the 70K U1 snRNP protein. Cell, 1989, 57, 89–101.

Kobe, B. and Kajava, A. V., The leucine-rich repeat as a protein recognition motif. Curr. Opin. Struct. Biol., 2001, 11, 725–732.

Kramer, A., Mulhauser, F., Wersig, C., Groning, K. and Bilbe, G., Mammalian splicing factor SF3a120 represents a new member of the SURP family of proteins and is homologous to the essential splicing factor Prp21p of Saccharomyces cerevisiae. RNA, 1995, 1, 260–272.

Kuwasako, K., He, F., Inoue, M., Tanaka, A., Sugano, S., Guntert, P., Muto, Y. and Yokoyama, S., Solution structures of the SURP domains and the subunit-assembly mechanism within the splicing factor SF3a complex in 17S U2 snRNP. Structure, 2006, 14, 1677–1689.

Will, C. L., Urlaub, H., Achsel, T., Gentzel, M., Wilm, M. and Luhrmann, R., Characterization of novel SF3b and 17S U2 snRNP proteins, including a human Prp5p homologue and an SF3b dead-box protein. EMBO. J., 2002, 21, 4978–4988.

Trappe, R., Ahmed, M., Glaser, B., Vogel, C., Tascou, S., Burfeind, P. and Engel, W., Identification and characterization of a novel murine multigene family containing a PHD-finger-like motif. Biochem. Biophys. Res. Commun., 2002, 293, 816–826.

Hryciw, T., Tang, M., Fontanie, T. and Xiao, W., MMS1 protects against replication-dependent DNA damage in saccharomyces cerevisiae. Mol. Genet. Genomics, 2002, 266, 848–857.

Li, Y., Chen, Z. Y., Wang, W., Baker, C. C. and Krug, R. M., The 3'-end-processing factor CPSF is required for the splicing of singleintron pre-mRNAS in vivo. RNA, 2001, 7, 920–931.

Freund, C., Dotsch, V., Nishizawa, K., Reinherz, E. L. and Wagner, G., The GYF domain is a novel structural fold that is involved in lymphoid signaling through proline-rich sequences. Nat. Struct. Biol., 1999, 6, 656–660.

Nishizawa, K., Freund, C., Li, J., Wagner, G. and Reinherz, E. L., Identification of a proline-binding motif regulating CD2-triggered T lymphocyte activation. Proc. Natl. Acad. Sci. USA, 1998, 95, 14897–14902.

Reuter, K., Nottrott, S., Fabrizio, P., Luhrmann, R. and Ficner, R., Identification, characterization and crystal structure analysis of the human spliceosomal U5 snRNP-specific 15 KD protein. J. Mol. Biol., 1999, 294, 515–525.

Jermy, A. J., Willer, M., Davis, E., Wilkinson, B. M. and Stirling, C. J., The BRL domain in Sec63p is required for assembly of functional endoplasmic reticulum translocons. J. Biol. Chem., 2006, 281, 7899–7906.

Ponting, C. P., Proteins of the endoplasmic-reticulum-associated degradation pathway: Domain detection and function prediction. Biochem. J., 2000, 351(Pt 2), 527–535.

Aubourg, S., Kreis, M. and Lecharny, A., The dead box RNA helicase family in Arabidopsis thaliana. Nucleic Acids Res., 1999, 27, 628–636.

de la Cruz, J., Kressler, D. and Linder, P., Unwinding RNA in Saccharomyces cerevisiae: dead-box proteins and related families. Trends Biochem. Sci., 1999, 24, 192–198.

Urushiyama, S., Tani, T. and Ohshima, Y., Isolation of novel pre-mRNA splicing mutants of Schizosaccharomyces pombe. Mol. Gen. Genet, 1996, 253, 118–127.

Blatch, G. L. and Lassle, M., The tetratricopeptide repeat: a structural motif mediating protein–protein interactions. Bioessays, 1999, 21, 932–939.

Staub, E., Fiziev, P., Rosenthal, A. and Hinzmann, B., Insights into the evolution of the nucleolus by an analysis of its protein domain repertoire. Bioessays, 2004, 26, 567–581.

Ritchie, D. B., Schellenberg, M. J., Gesner, E. M., Raithatha, S. A., Stuart, D. T. and Macmillan, A. M., Structural elucidation of a Prp8 core domain from the heart of the spliceosome. Nat. Struct. Mol. Biol., 2008, 15, 1199–1205.

Ayadi, L., Callebaut, I., Saguez, C., Villa, T., Mornon, J. P. and Banroques, J., Functional and structural characterization of the Prp3 binding domain of the yeast Prp4 splicing factor. J. Mol. Biol., 1998, 284, 673–687.

Wang, P. and Heitman, J., The cyclophilins. Genome Biol., 2005, 6, 226.

Stirnimann, C. U., Petsalaki, E., Russell, R. B. and Muller, C. W., WD40 proteins propel cellular networks. Trends Biochem. Sci., 2010, 35, 565–574.

Weidenhammer, E. M., Singh, M., Ruiz-Noriega, M. and Wool-ford Jr., J. L., The Prp31 gene encodes a novel protein required for pre-mRNA splicing in Saccharomyces cerevisiae. Nucleic Acids Res., 1996, 24, 1164–1170.

Wilkinson, C. R., Dittmar, G. A., Ohi, M. D., Uetz, P., Jones, N. and Finley, D., Ubiquitin-like protein HUB1 is required for pre-mRNA splicing and localization of an essential splicing factor in fission yeast. Curr. Biol., 2004, 14, 2283–2288.

Hershko, A. and Ciechanover, A., The ubiquitin system. Annu. Rev. Biochem., 1998, 67, 425–479.

Wilkinson, K. D., Regulation of ubiquitin-dependent processes by deubiquitinating enzymes. FASEB J., 1997, 11, 1245–1256.

Grillari, J. et al., SNEV is an evolutionarily conserved splicing factor whose oligomerization is necessary for spliceosome assembly. Nucleic Acids Res., 2005, 33, 6868–6883.

Ohi, M. D., Link, A. J., Ren, L., Jennings, J. L., McDonald, W. H. and Gould, K. L., Proteomics analysis reveals stable multiprotein complexes in both fission and budding yeasts containing Myb-related Cdc5p/Cef1p, novel pre-mRNA splicing factors, and snR-NAS. Mol. Cell Biol., 2002, 22, 2011–2024.

Dix, I., Russell, C., Yehuda, S.B., Kupiec, M. and Beggs, J. D., The identification and characterization of a novel splicing protein, Isy1p of Saccharomyces cerevisiae. RNA, 1999, 5, 360–368.

Shepard, P. J. and Hertel, K. J., The SR protein family. Genome Biol., 2009, 10, 242.

Kempken, F., Alternative splicing in ascomycetes. Appl. Microbiol. Biotechnol., 2013, 97, 4235–4241.

Sauliere, J., Haque, N., Harms, S., Barbosa, I., Blanchette, M. and Le Hir, H., The exon junction complex differentially marks spliced junctions. Nat. Struct. Mol. Biol., 2010, 17, 1269–1271.

Bordonne, R., Banroques, J., Abelson, J. and Guthrie, C., Domains of yeast U4 spliceosomal RNA required for Prp4 protein binding, snRNP–snRNP interactions, and pre-mRNA splicing in vivo. Genes Dev., 1990, 4, 1185–1196.

Galej, W. P., Oubridge, C., Newman, A. J. and Nagai, K., Crystal structure of Prp8 reveals active site cavity of the spliceosome. Nature, 2013, 493, 638-+.

Kondo, Y., Oubridge, C., van Roon, A. M. M. and Nagai, K., Crystal structure of human U1 snRNP, a small nuclear ribonucleo-protein particle, reveals the mechanism of 5 splice site recognition. Elife, 2015, 4.

Korneta, I., Magnus, M. and Bujnicki, J. M., Structural bioinformatics of the human spliceosomal proteome. Nucleic Acids Res., 2012, 40, 7046–7065.

Alpha Particle X-ray Spectrometer onboard Chandrayaan-2 Rover

Abstract Views :258 | PDF Views:82

Authors

M. Shanmugam ¹, S. V. Vadawale ¹, Arpit R. Patel ¹, N. P. S. Mithun ¹, Hitesh Kumar Adalaja ¹, Tinkal Ladiya ¹, Shiv Kumar Goyal ¹, Neeraj K. Tiwari ¹, Nishant Singh ¹, Sushil Kumar ¹, Deepak Kumar Painkra ¹, A. K. Hait ², A. Patinge ², Abhishek Kumar ³, Saleem Basha ³, Vivek R. Subramanian ³, R. G. Venkatesh ³, D. B. Prashant ³, Sonal Navle ³, Y. B. Acharya ¹, S. V. S. Murty ¹, Anil Bhardwaj ¹

Affiliations
1 Physical Research Laboratory, Ahmedabad 380 009, IN
2 Space Applications Centre, Ahmedabad 380 015, IN
3 U.R. Rao Satellite Centre, Bengaluru 560 017, IN

Source

Current Science, Vol 118, No 1 (2020), Pagination: 53-61

Abstract

Alpha Particle X-ray Spectrometer (APXS) is one of the two scientific experiments on Chandrayaan-2 rover named as Pragyan. The primary scientific objective of APXS is to determine the elemental composition of the lunar surface in the surrounding regions of the landing site. This will be achieved by employing the technique of X-ray fluorescence (XRF) spectroscopy using in situ excitation source ²⁴⁴Cm emitting both X-rays and alpha particles. These radiations excite characteristic X-rays of the elements by the processes of particle induced X-ray emission and XRF. The characteristic X-rays are detected by the ‘state-of-the-art’ X-ray detector known as Silicon Drift Detector, which provides high energy resolution, as well as high efficiency in the energy range of 1–25 keV. This enables APXS to detect all major rock forming elements such as, Na, Mg, Al, Si, Ca, Ti and Fe. The flight model of the APXS payload has been completed and tested for various instrument parameters. The APXS provides energy resolution of ~135 eV at 5. 9keV for the detector operating temperature of about –35°C. The design details and the performance measurement of APXS are presented in this paper.

Keywords

Alpha Particle X-Ray Spectrometer, CSPA, Silicon Drift Detector, X-Ray Spectrometer.

Full Text

References

McSween, H. Y. and Huss, G. R., Cosmochemistry, Cambridge University Press, Cambridge, 2010.

Laxmiprasad, A. S. et al., An in situ laser induced breakdown spectroscope (LIBS) for Chandrayaan-2 rover: ablation kinetics and emissivity estimates. Adv. Space Res., 2013, 52, 332–341.

Rieder, R. et al., Determination of the chemical composition of Martian soil and rocks: the alpha proton X-ray spectrometer. J. Geophys. Res., 1997, 102, 4027–4044.

Rieder, R. et al., The new Athena alpha particle X-ray spectrometer for the Mars Exploration Rovers. J. Geophys. Res.: (Planets), 2003, 108, 8066.

Gellert, R. et al., The alpha-particle X-ray spectrometer (APXS) for the mars science laboratory (MSL) rover mission. Lunar and Planetary Science Conference, abstract no. 2364, 2009.

Bridges, N. T., Crisp, J. A. and Bell, J. F., Characteristics of the pathfinder APXS sites: implications for the composition of Martian rocks and soils. J. Geophys. Res., 2001, 106, 14621–14665.

Gellert, R. et al., Alpha particle X-ray spectrometer (APXS): results from Gusev crater and calibration report. J. Geophys. Res., 2006, 111; E02S05; doi:10.1029/2005JE002555.

O’Connell-Cooper, C. D. et al., APXS derived chemistry of the Bagnold dune sands: comparisons with gale crater soils and the global Martian average. J. Geophys. Res.: Planets, 2017, 122, 2623–2643.

Klingelhofer, G. et al., The Rosetta alpha particle X-ray spectrometer (APXS). Space Sci. Rev., 2007, 128, 383–396.

Turkevich, A. L., Franzgrote, E. J. and Patterson, J. H., Chemical analysis of the moon at the surveyor 5 landing site. Science, 1967, 158, 635–637.

Chunlai, L. et al., The Chang’e 3 mission overview. Space Sci. Rev., 2015, 190, 85–101.

Ye, P. J. et al., An overview of the mission and technical characteristics of Chang’e 4 lunar probe. Sci. China Technol. Sci., 2017, 60, 658–667.

Zhang, G.-L. et al., Laboratory verification of the active particleinduced X-ray spectrometer (APXS) on the Chang’e-3 mission. Res. Astron. Astrophys., 2015, 15, 1893.

Shanmugam, M. et al., Alpha particle X-ray spectrometer (APXS) onboard Chandrayaan-2 rover. Adv. Space Res., 2014, 54, 1974– 1986.

Goyal, S. K. et al., Laboratory XRF measurements using alpha particle X-ray spectrometer of Chandrayaan-2 rover: comparison with GEANT4 simulation results. IEEE proc. NSS/MIC/RTSD1695, 2013.

Radchenko, V. M. and Ryabinin, M. A., Research sources of ionizing radiation based on transplutonium elements, IOP Conference Series: Materials Science and Engineering, 2010.

Fine Root Biomass Differs Significantly across Different Forest Types and Soil Depth in Central Himalaya, India

Abstract Views :225 | PDF Views:100

Authors

Harish Bahadur Chand ¹, Ganesh Joshi ², Roshan Prasad Bhatta ³, Sanjay Singh ⁴, Abhishek Kumar ¹, Nabin Raj Joshi ⁵, Ramesh Bohara ²

Affiliations
1 Forest Research Institute (Deemed to be University), Dehradun 248 001, IN
2 Department of Forestry and Environmental Science, Kumaun University, Nainital 263 001, IN
3 Institute of Forestry, Pokhara 33700, NP
4 Indian Council of Forestry Research and Education, Dehradun 248 001, IN
5 Asia Network for Sustainable Agriculture and Bioresources, Kathmandu 44600, NP

Source

Current Science, Vol 123, No 2 (2022), Pagination: 194-201

Abstract

Fine roots (diameter less than 2 mm) comprise a significant portion of the plant biomass. They are important for water absorption, cycling of nutrients and the carbon budget on a global scale. The aim of the present study was to quantify fine root biomass in the Nainital district, Central Himalaya, India, which has several dominant forest types. A total of 81 samples were collected from nine sample plots for each forest type in three distinct directions. The results showed that sal forest (1.11  0.04 t ha–1) had the largest fine root biomass, followed by oak forest (0.72  0.06 t ha–1) and pine forest (0.61  0.06 t ha–1). We observed that the trend in fine root biomass across different forest types was as follows: sal forest > oak forest > pine forest, significant at 0.05 level. Fine root biomass was also observed to decrease similarly with increasing soil depth in each forest type, following the trend: 0–20 cm > 20– 40 cm > 40–60 cm, which was significant at 0.05 level. Researchers will benefit from this study since it will help them comprehend fine root biomass variation and offer baseline data for future research on nutrient cycling and the global carbon budget.

Keywords

Forest Types, Global Carbon Budget, Nutrient Cycling, Plant Biomass, Soil Depth

Full Text

References

Sayer, E. J., Tanner, E. V. J. and Cheesman, A. W., Increased litterfall changes fine root distribution in a moist tropical forest. Plant Soil, 2006, 281, 5–13.

Vogt, K. A., Vogt, D. J., Palmiotto, P. A., Boon, P., Ohara, J. and Asbjornsen, H., Review of root dynamics in forest ecosystems grouped by climate, climatic forest type and species. Plant Soil, 1996, 187, 159–219.

Gill, A. R. and Jackson, B. R., Global patterns of root turnover for terrestrial ecosystems. New Phytol., 2000, 147, 13–31.

Vogt, K. A., Grier, C. C. and Vogt, D. J., Production, turnover, and nutrient dynamics of above- and belowground detritus of world forests. Adv. Ecol. Res., 1986, 15, 303–378.

Persson, H., The distribution and productivity of fine roots in boreal forests. Plant Soil, 1982, 71, 87–101.

Noordwijik, M., Lawson, G., Soumare, A., Groot, J. J. R. and Hairiah, K., Root distribution of trees and crops: competition and/or complementarit. In Tree-Crop Interactions: A Physiological Approach (eds On, C. K. and Huxley, P.), CAB International, Washington, Oxon, UK, 1996, pp. 319–364.

Jackson, R. B., Mooney, H. A. and Schulze, E. D., A global budget for fine roots biomass, surface area, and nutrient contents. Proc. Natl. Acad. Sci. USA, 1997, 94, 7362–7366.

Jones, R. H., Mitchell, R. J., Stevens, G. N. and Pecot, S. D., Controls of fine root dynamics across a gradient of gap sizes in a pine woodland. Oecologia, 2003, 134, 132–143.

Hendrick, R. L. and Pregitzer, K. S., Patterns of fine root mortality in 2 sugar maple forests. Nature, 1993, 361, 59–61.

Wang, Z. Q. and Guo, D. L., Root ecology. J. Plant Ecol., 2008, 32, 1213–1216.

Barbhuiya, A. R., Arunachalam, A., Pandey, H. N., Khan, M. L. and Arunachalam, K., Fine root dynamics in undisturbed and disturbed stands of a tropical wet evergreen forest in northeast India. Trop. Ecol., 2012, 53(1), 69–79.

Pant, H. and Tewari, A., Fine root biomass, productivity and turnover in two contrasting aspects in natural chir pine (Pinus roxburghii Sarg.) forests of Central Himalaya. Russ. J. Ecol., 2015, 46(6), 511– 517.

Welke, S. E., Hope, G. D. and Hunt, G. A., Effects of harvesting on fine root biomass and decomposition in an Engelmann spruce subalpine fir forest. Can. J. For. Res., 2003, 33(5), 847–853.

Polomski, O. and Kuhn, N., Wurzelsysteme Forschungsanstalt für Wald. In Schnee und Landschaft (WSL/FNP) Birmensdorf (ed. Haupt, P.), Bern, Switzerland, 1998.

Steen, E., Root and rhizome dynamics in a perennial grass crop during an annual growth cycle. Swed. J. Agric. Res., 1985, 156, 25–30.

Eissenstat, D. M. and Yanai, R. D., The ecology of root life span. Adv. Ecol. Res., 1997, 27, 1–62.

Vogt, K. A., Vogt, D. J. and Bloomfield, J., Analysis of some direct and indirect methods for estimating roots biomass and production of forests at an ecosystem level. Plant Soil, 1998, 200, 71–89.

Sabin, T. P., Krishnan, R., Vellore, R., Priya, P., Borgaonkar, H. P., Singh, B. B. and Sagar, A., Climate change over the Himalayas. In Assessment of Climate Change over the Indian Region (eds Krishnan, R. et al.), Springer, Singapore, 2020, pp. 207–222.

Yuan, Z. Y. and Chen, H. Y. H., Fine root biomass, production, turnover rates, and nutrient contents in boreal forest ecosystems in relation to species, climate, fertility, and stand age: literature review and meta-analyses. Crit. Rev. Plant Sci., 2010, 29, 204–221.

Persson, H., Root dynamics in a young Scots pine stand in Central Sweden. Oikos, 1978, 30, 508–519.

Usman, S., Rawat, Y. S., Singh, S. P. and Gargoti, S. C., Fine root biomass production and turnover in evergreen forests of Central Himalaya, India. Oecologia, 1997, 6, 4–8.

Ostonen, I., Lohmus, K. and Pajuste, K., Fine root biomass, production and its proportion of NPP in a fertile middle-aged Norway spruce forest: comparison of soil core and ingrowth core methods. For. Ecol. Manage., 2005, 212, 264–277.

Bhattarai, P. K. and Mandal, N. T., Soil microbial biomass in relation to fine root in Kiteni hill Sal forest of Ilam, Eastern Nepal. Nepal J. Biosci., 2012, 2, 80–87.

Gautam, P. G. and Mandal, N., Effects of disturbance on fine root biomass in tropical moist forest of eastern Nepal. Nepal J. Biosci., 2012, 21, 10–16.

Leuschner, C. and Hertel, D., Fine root biomass of temperate forests in relation to soil acidity and fertility, climate, age and species. Prog. Bot., 2003, 64, 405–438.

Noguchi, H. et al., Fine root biomass in a tropical moist forest in the upper Negro River basin, Brazilian Amazon. Tropics, 2014, 22(4), 179–183.

Helmisaari, H. S., John, D., Pekka, N. and Mikko, K., Fine root biomass in relation to site and stand characteristics in Norway spruce and Scots pine stands. Tree Physiol., 2007, 27, 1493–1504.

Garkoti, S. C., Fine root dynamics in three central Himalayan high elevation forests ranging from closed canopied to open canopied tree line vegetation. J. For. Res., 2011, 16(2), 136–143.

Verma, A. K., Garkoti, S. C., Singh, S., Kumar, S. and Kumar, M., Fine root production and nutrient dynamics in relation to stand characteristics of chir pine mixed banj oak forests in Central Himalaya. Flora, 2021, 279, 151808.

Cordeiro, A. L. et al., Fine-root dynamics vary with soil depth and precipitation in a low-nutrient tropical forest in the Central Amazonia. Plant–Environ. Interact., 2020, 1(1), 3–16.

Melgar, R. J., Smyth, T. J., Sanchez, P. A. and Cravo, M. S., Fertilizer nitrogen movement in a Central Amazon Oxisol and Entisol cropped to corn. Fert. Res., 1992, 31, 241–252.

Pathak, G. C., Joshi, H., Singh, R. D., Tewari, A., Pandey, R. and Singh, S. P., Vertical root distribution in Himalayan trees: about half of roots occur below 30 cm, the generally sampled depth. Trop. Ecol., 2021, 62, 479–491.

Usman, S., Singh, S. P. and Rawat, Y. S., Fine root productivity and turnover in two evergreen Central Himalayan forests. Ann. Bot., 1999, 84, 87–94.

Rawat, S. V., Fine root biomass and soil nutrient in Van Panchayat forest of Almora district. Indian J. Plant Sci., 2012, 1(1), 101–108.

Nadelhoffer, K. J. and Raich, J. W., Fine root production estimates and belowground carbon allocation in forest ecosystems. Ecology, 1992, 73, 1139–1147.

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