CAO cDNA ORF clone, Arabidopsis thaliana(thale cress)

Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.
Lin X, Kaul S, Rounsley S, Shea TP, Benito MI, Town CD, Fujii CY, Mason T, Bowman CL, Barnstead M, Feldblyum TV, Buell CR, Ketchum KA, Lee J, Ronning CM, Koo HL, Moffat KS, Cronin LA, Shen M, Pai G, Van Aken S, Umayam L, Tallon LJ, Gill JE, Adams MD, Carrera AJ, Creasy TH, Goodman HM, Somerville CR, Copenhaver GP, Preuss D, Nierman WC, White O, Eisen JA, Salzberg SL, Fraser CM, Venter JC
Nature402(6763)761-8(1999 Dec)

CpSRP54 drives cpSRP43 to an active state, binding substrate in the H2O compartment. Bidentate interactions with Alb3 drive it to partial inactivity, selectively releasing LHCP transmembrane domains in a productive unloading complex at the membrane.
Title: Conformational dynamics of a membrane protein chaperone enables spatially regulated substrate capture and release.

cpSRP43 chromodomain 3 interacts with a linear motif in the Alb3 C-terminal tail. Study describes the structural basis for selectivity of CPSRP43 chromodomains 2 and 3 for their respective ligands cpSRP54 and Alb3.
Title: Structural basis for cpSRP43 chromodomain selectivity and dynamics in Alb3 insertase interaction.

results support the conclusion that substrate binding to the chloroplast SRP is modulated by protein structural dynamics in which a major role of cpSRP54 is to improve substrate binding efficiency to the cpSRP.
Title: Regulation of Structural Dynamics within a Signal Recognition Particle Promotes Binding of Protein Targeting Substrates.

A mechanism for recognition of the LHC aggregate by cpSRP43 elucidated by a biophysical and biochemical approach.
Title: Mechanism of an ATP-independent protein disaggregase: I. structure of a membrane protein aggregate reveals a mechanism of recognition by its chaperone.

The action of cpSRP43 can be dissected into two steps, initial recognition, during which cpSRP43 binds specifically to a recognition motif on the surface of the aggregate, followed by aggregate remodeling.
Title: Mechanism of an ATP-independent protein disaggregase: II. distinct molecular interactions drive multiple steps during aggregate disassembly.