RAF2 is a RuBisCO assembly factor in Arabidopsis thaliana

Autor: Laura M. Roy, Rebekka M. Wachter, Nicole M. Wheatley, Sabeeha S. Merchant, Rikard Fristedt, Jeremy Harbinson, David Kramer, Roberta Croce, Chen Hu, Linda J. Savage, Todd O. Yeates

Publikováno v: Plant Journal 94 (2018) 1
Fristedt, R, Hu, C, Wheatley, N, Roy, L M, Wachter, R M, Savage, L, Harbinson, J, Kramer, D M, Merchant, S S, Yeates, T & Croce, R 2018, ' RAF2 is a RuBisCO assembly factor in Arabidopsis thaliana ', Plant Journal, vol. 94, no. 1, pp. 146-156 . https://doi.org/10.1111/tpj.13849
Plant Journal, 94(1), 146-156. Wiley-Blackwell
Plant Journal, 94(1), 146-156

Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) catalyzes the reaction between gaseous carbon dioxide (CO2) and ribulose-1,5-bisphosphate. Although it is one of the most studied enzymes, the assembly mechanisms of the large hexadecameric Ru

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f73902fbd54b99552934d26c0f273909
https://doi.org/10.1111/tpj.13849

Structural characterization of the HSP70 interaction domain of the hepatitis C viral protein NS5A

Autor: Alan J. Waring, Asim Dasgupta, Ronik Khachatoorian, Chun-Ling Jung, Christopher Sundberg, Piotr Ruchala, Ekambaram Ganapathy, Samuel W. French, Vaithilingaraja Arumugaswami, Nicole M. Wheatley

Publikováno v: Khachatoorian, Ronik; Ruchala, Piotr; Waring, Alan; Jung, Chun-Ling; Ganapathy, Ekambaram; Wheatley, Nicole; et al.(2014). Structural characterization of the HSP70 interaction domain of the hepatitis C viral protein NS5A. Virology, 475, 46-55. UC Office of the President: Multicampus Research Programs and Initiatives (MRPI); a funding opportunity through UC Research Initiatives (UCRI). Retrieved from: http://www.escholarship.org/uc/item/91h66262

We previously identified the NS5A/HSP70 binding site to be a hairpin moiety at C-terminus of NS5A domain I and showed a corresponding cyclized polyarginine-tagged synthetic peptide (HCV4) significantly blocks virus production. Here, sequence comparis

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::535fc53a5bd54027b4c945b981950ba2
https://doi.org/10.1016/j.virol.2014.10.011

Putting the RuBisCO pieces together

Autor: Todd O. Yeates, Nicole M. Wheatley

Publikováno v: Science. 358:1253-1254

Among the thousands of different enzymes that have evolved in nature, ribulose-1,5-bisphosphate carboxylase-oxygenase (known as RuBisCO) holds a special place. It is the enzyme in plants, algae, and many photosynthetic bacteria that ultimately takes

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c00f5c1c4a68d5f855fd22203de3ad00
https://doi.org/10.1126/science.aar3107

Using comparative genomics to uncover new kinds of protein-based metabolic organelles in bacteria

Autor: Julien Jorda, David Lopez, Todd O. Yeates, Nicole M. Wheatley

Publikováno v: Protein Science. 22:179-195

Bacterial microcompartment (MCP) organelles are cytosolic, polyhedral structures consisting of a thin protein shell and a series of encapsulated, sequentially acting enzymes. To date, different microcompartments carrying out three distinct types of m

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::9b288136e7751e0625b4511c1efcb58e
https://doi.org/10.1002/pro.2196

Identification of a Unique Fe-S Cluster Binding Site in a Glycyl-Radical Type Microcompartment Shell Protein

Autor: Zhongyu Yang, Hoda Ahmed, Michael C. Thompson, Michael R. Sawaya, Nicole M. Wheatley, Julian P. Whitelegge, Soheil D. Gidaniyan, Julien Jorda, Krystal N. McCarty, Todd O. Yeates

Recently, progress has been made toward understanding the functional diversity of bacterial microcompartment (MCP) systems, which serve as protein-based metabolic organelles in diverse microbes. New types of MCPs have been identified, including the g

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a50ccf0de2e2cd30994057476aecdfa2
https://europepmc.org/articles/PMC4175982/