Dissection of Synechococcus rubisco large subunit sections involved in holoenzyme formation in Escherichia coli by combinatorial section swapping and sequence analyses
Engineering the CO2-fixing enzyme ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) to improve photosynthesis has long been sought. Rubisco large subunits (RbcL) are highly-conserved but because of certain undefined sequence differences, plant Rubisco research cannot fully utilise the robust...
Main Authors: | Yeap, Yee Hung, Koay, Teng Wei, Wong, Hann Ling, Lim, Boon Hoe |
---|---|
Format: | Article |
Language: | English |
Published: |
Penerbit Universiti Kebangsaan Malaysia
2018
|
Online Access: | http://journalarticle.ukm.my/12497/1/04%20Yee%20Hung%20Yeap.pdf |
Similar Items
-
Probing the rice Rubisco-Rubisco activase interaction via subunit heterooligomerization
by: Shivhare, Devendra, et al.
Published: (2021) -
Rubisco activase requires residues in the large subunit N terminus to remodel inhibited plant Rubisco
by: Ng, Jediael, et al.
Published: (2022) -
CaMKII autophosphorylation can occur between holoenzymes without subunit exchange
by: Iva Lučić, et al.
Published: (2023-08-01) -
A new role for proteins subunits of RNase P: stabilization of the telomerase holoenzyme
by: P. Daniela Garcia, et al.
Published: (2020-06-01) -
Binding Options for the Small Subunit-Like Domain of Cyanobacteria to Rubisco
by: Brandon A. Rohnke, et al.
Published: (2020-02-01)