The interaction between NFR and SYMRK initiates calcium spiking in the nucleus, presumably via a second messenger molecule.

Core symbiotic genes are activated.

Cytokinin signaling is initiated.

TLS Online TPP Program

#Id: 9280

#XL - Q Biochemistry

The interaction between NFR and SYMRK initiates calcium spiking in the nucleus, presumably via a second messenger molecule.

Core symbiotic genes are activated.

Cytokinin signaling is initiated.

TLS Online TPP Program

#Id: 9280

#XL - S Microbiology

The interaction between NFR and SYMRK initiates calcium spiking in the nucleus, presumably via a second messenger molecule.

Core symbiotic genes are activated.

Cytokinin signaling is initiated.

TLS Online TPP Program

#Id: 7938

#XL - Q Biochemistry

The SRP and the nascent polypeptide chain–ribosome complex bind to the SRP receptor in the ER membrane. This interaction is strengthened by the binding of GTP to both the SRP and its receptor.

TLS Online TPP Program

#Id: 7937

#XL - Q Biochemistry

Once the ER signal sequence emerges from the ribosome, it is bound by a signal recognition particle (SRP)

TLS Online TPP Program

#Id: 7936

#XL - Q Biochemistry

The SRP is made up of six proteins bound to a 300-nucleotide RNA, which acts as a scaffold for the hexamer.

TLS Online TPP Program

#Id: 7935

#XL - Q Biochemistry

The SRP is a cytosolic ribonucleoprotein particle that transiently binds to both the ER signal sequence in a nascent protein and the large (60S) ribosomal subunit, forming a large complex.

TLS Online TPP Program

#Id: 7934

#XL - Q Biochemistry

The two key components in protein targeting in ER:

Signal recognition particle (SRP)

SRP receptor

TLS Online TPP Program

#Id: 7933

#XL - Q Biochemistry

Signal sequences

contain one or more positively charged amino acids adjacent to a continuous stretch of 6–12 hydrophobic residues (known as the hydrophobic core)