Bhalchandra Jadhav
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Previous Organizations / Institutes
The organizations / institutes from the scholar's other articles in the past ten years
Research Subjects
Bhalchandra Jadhav has a total of 6 co-authors. Here are the top co-authors by number of shared publications:
- Irmgard Sinning
Heidelberg University Biochemistry Center (BZH), Im Neuenheimer Feld 328, 69120 Heidelberg, Germany
2 shared publications - Martin R. Pool
Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, England, UK
2 shared publications - Klemens Wild
Heidelberg University Biochemistry Center, INF328, D-69120 Heidelberg, Germany
1 shared publication - Michael McKenna
Department of Cell Biology, Harvard Medical School, 240 Longwood Ave., Boston, MA 02115, USA
1 shared publication - Nicholas Johnson
Institute of Organic Chemistry and Biochemistry, Czech Academy of Science, Prague, Czech Republic
1 shared publication - Stephen High
Division of Molecular and Cellular Function, Faculty of Biology, Medicine and Health, University of Manchester
1 shared publication
Latest Publications
- Open Access
- 4 December 2015
- Published by Springer Nature in Nature Communications
- Vol. 6 (1) , 10133
Mammalian SRP receptor switches the Sec61 translocase from Sec62 to SRP-dependent translocation
Two distinct pathways deliver secretory proteins to the Sec61 protein translocase in the endoplasmic reticulum membrane. The canonical pathway requires the signal recognition particle (SRP) and its cognate receptor (SR), and targets ribosome-associated proteins to the Sec translocase. The SRP-independent pathway requires the Sec translocase-associated ER membrane protein Sec62 and can be uncoupled from translation. Here we show that SR switches translocons to SRP-dependent translocation by displacing Sec62. This activity localizes to the charged linker region between the longin and GTPase domains of SRα. Using truncation variants, crosslinking and translocation assays reveals two elements with distinct functions as follows: one rearranges the translocon, displacing Sec62 from Sec61. A second promotes ribosome binding and is conserved between all eukaryotes. These specific regions in SRα reprogramme the Sec translocon and facilitate recruitment of ribosome-nascent chain complexes. Overall, our study identifies an important function of SR, which mechanistically links two seemingly independent modes of translocation.
- 4 December 2015
- Published by Springer Nature in Nature Communications
- Vol. 6 (1) , 10133
Open AccessMammalian SRP receptor switches the Sec61 translocase from Sec62 to SRP-dependent translocation
Two distinct pathways deliver secretory proteins to the Sec61 protein translocase in the endoplasmic reticulum membrane. The canonical pathway requires the signal recognition particle (SRP) and its cognate receptor (SR), and targets ribosome-associated proteins to the Sec translocase. The SRP-independent pathway requires the Sec translocase-associated ER membrane protein Sec62 and can be uncoupled from translation. Here we show that SR switches translocons to SRP-dependent translocation by displacing Sec62. This activity localizes to the charged linker region between the longin and GTPase domains of SRα. Using truncation variants, crosslinking and translocation assays reveals two elements with distinct functions as follows: one rearranges the translocon, displacing Sec62 from Sec61. A second promotes ribosome binding and is conserved between all eukaryotes. These specific regions in SRα reprogramme the Sec translocon and facilitate recruitment of ribosome-nascent chain complexes. Overall, our study identifies an important function of SR, which mechanistically links two seemingly independent modes of translocation.
Structure and Switch Cycle of SRβ as Ancestral Eukaryotic GTPase Associated with Secretory Membranes