CPFTSY 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)

cpFtsY membrane-binding motif plays a critical role in the intramolecular communication that regulates cpSRP receptor functions at the membrane.
Title: The membrane-binding motif of the chloroplast signal recognition particle receptor (cpFtsY) regulates GTPase activity.

cpftsY mutants generally exhibit defects in the biogenesis of light-harvesting chlorophyll proteins and other thylakoidal membrane proteins that are less severe than in the alb3 mutants.
Title: Non-identical contributions of two membrane-bound cpSRP components, cpFtsY and Alb3, to thylakoid biogenesis.

the crystal structure of chloroplast FtsY (cpFtsY) at 1.75 A resolution.
Title: The structure of the chloroplast signal recognition particle (SRP) receptor reveals mechanistic details of SRP GTPase activation and a conserved membrane targeting site.

These results highlight intriguing differences between the classical and chloroplast SRP and SRP receptor GTPases, and help explain how the chloroplast SRP pathway can mediate efficient targeting of proteins to the thylakoid membrane.
Title: Efficient interaction between two GTPases allows the chloroplast SRP pathway to bypass the requirement for an SRP RNA.

Mutations within the cpFtsY gene are associated with an inability to induce Fe(III) chelate reductase activity in response to iron deficiency.
Title: Arabidopsis cpFtsY mutants exhibit pleiotropic defects including an inability to increase iron deficiency-inducible root Fe(III) chelate reductase activity.