In the article by Dahong Chen, Chunjing Qu, and Randall S. Hewes (GENETICS 197: 1267–1283) entitled “Neuronal Remodeling During Metamorphosis is Regulated by the alan shepard (shep) Gene in Drosophila melanogaster,” Sonia M. Bjorum and Kathleen M. Beckingham were unintentionally omitted from the author list. This has been corrected, and the author list and affiliations should read as shown below:
Dahong Chen,* Chunjing Qu,*,1 Sonia M. Bjorum,†,2 Kathleen M. Beckingham,† and Randall S. Hewes*,3
*Department of Biology, University of Oklahoma, Norman, Oklahoma 73019, and †Department of Biochemistry and Cell Biology, Rice University, Houston, Texas 77005
1Present address: Baylor College of Medicine, Houston, TX 77030.
2Present address: American Type Culture Collection, Manassas, VA 20110.
3Corresponding author: Department of Biology, University of Oklahoma, 730 Van Vleet Oval, Room 314, Norman, OK 73019. E-mail: hewes@ou.edu
The following reference was added to the introduction on page 1268 and literature cited:
Bjorum, S. M., 2006 Two genes affecting Drosophila gravitaxis. Annual Drosophila Research Conference 47: Abstract 615B.
The following text was deleted on page 1268 from the Materials and Methods:
(provided by K. Beckingham, Rice University)
The following text was added to the Results in the last paragraph on page 1275:
generated against a unique region common to all SHEP isoforms
The following text replaced or was added to the Acknowledgments:
“Kathleen Beckingham (Rice University) for the anti-SHEP antiserum,” was replaced with “Rebecca A. Simonette for expert assistance in preparation of the SHEP antibody,”. The text, “and to K.M.B. from NASA (NNX09AH43G)”, was added.
The following additional details were added to the Material and Methods section:
Antibody generation
A 117-amino-acid region of SHEP, common to all isoforms of the protein and showing no significant similarity to any other protein in the D. melanogaster genome, was chosen for antibody generation. This region is C-terminal to the two RNA Recognition Motifs (RRM-MSSPs) of SHEP and begins at residue 447 after the ATG start site in SHEP protein isoform PA (see Flybase http://flybase.org). Primers that add an upstream EcoRI site (5′-ATCGAATTCCAGGTGGGTGGCTATCCAGTG-3′) and a downstream XhoI site (5′-TGACTCGAGTGATGCAGCTGTGCTAGCCTGTT-3′) were used to generate the required PCR fragment from the shep cDNA clone LD29922 (Berkeley Drosophila Genome Project). After initial cloning into pCR4-TOPO (Invitrogen), the coding region was transferred to expression vector pGEX-6P-1 as an EcoRI/XhoI fragment to generate a GST-shep fused coding sequence. After induction, a fusion protein was collected on a glutathione column. The SHEP region was released by cleavage with PreScission Protease (GE Life Sciences) and used to raise antibodies in a rabbit (Cocalico Biologicals, Inc.).